Localization-specific distributions of protein pI in human proteome are governed by local pH and membrane charge
Background Whole-proteome distributions of protein isoelectric point (pI) values in different organisms are bi- or trimodal with some variations. It was suggested that the observed multimodality of the proteome-wide pI distributions is associated with subcellular localization-specific differences in...
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| Autor*in: |
Kurotani, Atsushi [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2019 |
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| Schlagwörter: |
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| Anmerkung: |
© The Author(s). 2019 |
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| Übergeordnetes Werk: |
Enthalten in: BMC cell biology - London : BioMed Central, 2000, 20(2019), 1 vom: 20. Aug. |
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| Übergeordnetes Werk: |
volume:20 ; year:2019 ; number:1 ; day:20 ; month:08 |
| Links: |
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| DOI / URN: |
10.1186/s12860-019-0221-4 |
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SPR026940620 |
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| 520 | |a Background Whole-proteome distributions of protein isoelectric point (pI) values in different organisms are bi- or trimodal with some variations. It was suggested that the observed multimodality of the proteome-wide pI distributions is associated with subcellular localization-specific differences in the local pI distributions. However, the factors responsible for variation of the intracellular localization-specific pI profiles have not been investigated in detail. Results In this work, we explored proteome-wide pI distributions of 32,138 human proteins predicted to reside in 10 subcellular compartments, as well as the pI distributions of experimentally observed lysosomal and Golgi proteins. The distributions were found to differ significantly, although all of them adhered to the major recurrent bimodal pattern. Grossly, acid-biased and alkaline-biased patterns with various minor statistical features were observed at different subcellular locations. Bioinformatics analysis revealed the existence of strong statistically significant correlations between protein pI and subcellular localization. Most markedly, protein pI was found to correlate positively with nuclear and mitochondrial locations and negatively with cytoskeletal, cytoplasmic, lysosomal and peroxisomal environment. Further analysis demonstrated that subcellular compartment-specific pI distributions are greatly influenced by local pH and organelle membrane charge. Multiple nonlinear regression analysis identified a polynomial function of the two variables that best fitted the mean pI values of the localization-specific pI distributions. A high coefficient of determination calculated for this regression (R2 = 0.98) suggests that local pH and organelle membrane charge are the major factors responsible for variation of the intracellular localization-specific pI profiles. Conclusions Our study demonstrates that strong correlations exist between protein pI and subcellular localization. The specific pI distributions at different subcellular locations are defined by local environment. Predominantly, it is the local pH and membrane charge that shape the organelle-specific protein pI patterns. These findings expand our understanding of spatial organization of the human proteome. | ||
| 650 | 4 | |a Bioinformatics |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Human proteome |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Protein pI |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Protein localization |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Regression analysis |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Tokmakov, Alexander A. |4 aut | |
| 700 | 1 | |a Sato, Ken-Ichi |4 aut | |
| 700 | 1 | |a Stefanov, Vasily E. |4 aut | |
| 700 | 1 | |a Yamada, Yutaka |4 aut | |
| 700 | 1 | |a Sakurai, Tetsuya |4 aut | |
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10.1186/s12860-019-0221-4 doi (DE-627)SPR026940620 (SPR)s12860-019-0221-4-e DE-627 ger DE-627 rakwb eng Kurotani, Atsushi verfasserin aut Localization-specific distributions of protein pI in human proteome are governed by local pH and membrane charge 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s). 2019 Background Whole-proteome distributions of protein isoelectric point (pI) values in different organisms are bi- or trimodal with some variations. It was suggested that the observed multimodality of the proteome-wide pI distributions is associated with subcellular localization-specific differences in the local pI distributions. However, the factors responsible for variation of the intracellular localization-specific pI profiles have not been investigated in detail. Results In this work, we explored proteome-wide pI distributions of 32,138 human proteins predicted to reside in 10 subcellular compartments, as well as the pI distributions of experimentally observed lysosomal and Golgi proteins. The distributions were found to differ significantly, although all of them adhered to the major recurrent bimodal pattern. Grossly, acid-biased and alkaline-biased patterns with various minor statistical features were observed at different subcellular locations. Bioinformatics analysis revealed the existence of strong statistically significant correlations between protein pI and subcellular localization. Most markedly, protein pI was found to correlate positively with nuclear and mitochondrial locations and negatively with cytoskeletal, cytoplasmic, lysosomal and peroxisomal environment. Further analysis demonstrated that subcellular compartment-specific pI distributions are greatly influenced by local pH and organelle membrane charge. Multiple nonlinear regression analysis identified a polynomial function of the two variables that best fitted the mean pI values of the localization-specific pI distributions. A high coefficient of determination calculated for this regression (R2 = 0.98) suggests that local pH and organelle membrane charge are the major factors responsible for variation of the intracellular localization-specific pI profiles. Conclusions Our study demonstrates that strong correlations exist between protein pI and subcellular localization. The specific pI distributions at different subcellular locations are defined by local environment. Predominantly, it is the local pH and membrane charge that shape the organelle-specific protein pI patterns. These findings expand our understanding of spatial organization of the human proteome. Bioinformatics (dpeaa)DE-He213 Human proteome (dpeaa)DE-He213 Protein pI (dpeaa)DE-He213 Protein localization (dpeaa)DE-He213 Regression analysis (dpeaa)DE-He213 Tokmakov, Alexander A. aut Sato, Ken-Ichi aut Stefanov, Vasily E. aut Yamada, Yutaka aut Sakurai, Tetsuya aut Enthalten in BMC cell biology London : BioMed Central, 2000 20(2019), 1 vom: 20. Aug. (DE-627)326644830 (DE-600)2041486-9 1471-2121 nnns volume:20 year:2019 number:1 day:20 month:08 https://dx.doi.org/10.1186/s12860-019-0221-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_22 GBV_ILN_2003 GBV_ILN_2008 GBV_ILN_2021 GBV_ILN_4305 AR 20 2019 1 20 08 |
| spelling |
10.1186/s12860-019-0221-4 doi (DE-627)SPR026940620 (SPR)s12860-019-0221-4-e DE-627 ger DE-627 rakwb eng Kurotani, Atsushi verfasserin aut Localization-specific distributions of protein pI in human proteome are governed by local pH and membrane charge 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s). 2019 Background Whole-proteome distributions of protein isoelectric point (pI) values in different organisms are bi- or trimodal with some variations. It was suggested that the observed multimodality of the proteome-wide pI distributions is associated with subcellular localization-specific differences in the local pI distributions. However, the factors responsible for variation of the intracellular localization-specific pI profiles have not been investigated in detail. Results In this work, we explored proteome-wide pI distributions of 32,138 human proteins predicted to reside in 10 subcellular compartments, as well as the pI distributions of experimentally observed lysosomal and Golgi proteins. The distributions were found to differ significantly, although all of them adhered to the major recurrent bimodal pattern. Grossly, acid-biased and alkaline-biased patterns with various minor statistical features were observed at different subcellular locations. Bioinformatics analysis revealed the existence of strong statistically significant correlations between protein pI and subcellular localization. Most markedly, protein pI was found to correlate positively with nuclear and mitochondrial locations and negatively with cytoskeletal, cytoplasmic, lysosomal and peroxisomal environment. Further analysis demonstrated that subcellular compartment-specific pI distributions are greatly influenced by local pH and organelle membrane charge. Multiple nonlinear regression analysis identified a polynomial function of the two variables that best fitted the mean pI values of the localization-specific pI distributions. A high coefficient of determination calculated for this regression (R2 = 0.98) suggests that local pH and organelle membrane charge are the major factors responsible for variation of the intracellular localization-specific pI profiles. Conclusions Our study demonstrates that strong correlations exist between protein pI and subcellular localization. The specific pI distributions at different subcellular locations are defined by local environment. Predominantly, it is the local pH and membrane charge that shape the organelle-specific protein pI patterns. These findings expand our understanding of spatial organization of the human proteome. Bioinformatics (dpeaa)DE-He213 Human proteome (dpeaa)DE-He213 Protein pI (dpeaa)DE-He213 Protein localization (dpeaa)DE-He213 Regression analysis (dpeaa)DE-He213 Tokmakov, Alexander A. aut Sato, Ken-Ichi aut Stefanov, Vasily E. aut Yamada, Yutaka aut Sakurai, Tetsuya aut Enthalten in BMC cell biology London : BioMed Central, 2000 20(2019), 1 vom: 20. Aug. (DE-627)326644830 (DE-600)2041486-9 1471-2121 nnns volume:20 year:2019 number:1 day:20 month:08 https://dx.doi.org/10.1186/s12860-019-0221-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_22 GBV_ILN_2003 GBV_ILN_2008 GBV_ILN_2021 GBV_ILN_4305 AR 20 2019 1 20 08 |
| allfields_unstemmed |
10.1186/s12860-019-0221-4 doi (DE-627)SPR026940620 (SPR)s12860-019-0221-4-e DE-627 ger DE-627 rakwb eng Kurotani, Atsushi verfasserin aut Localization-specific distributions of protein pI in human proteome are governed by local pH and membrane charge 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s). 2019 Background Whole-proteome distributions of protein isoelectric point (pI) values in different organisms are bi- or trimodal with some variations. It was suggested that the observed multimodality of the proteome-wide pI distributions is associated with subcellular localization-specific differences in the local pI distributions. However, the factors responsible for variation of the intracellular localization-specific pI profiles have not been investigated in detail. Results In this work, we explored proteome-wide pI distributions of 32,138 human proteins predicted to reside in 10 subcellular compartments, as well as the pI distributions of experimentally observed lysosomal and Golgi proteins. The distributions were found to differ significantly, although all of them adhered to the major recurrent bimodal pattern. Grossly, acid-biased and alkaline-biased patterns with various minor statistical features were observed at different subcellular locations. Bioinformatics analysis revealed the existence of strong statistically significant correlations between protein pI and subcellular localization. Most markedly, protein pI was found to correlate positively with nuclear and mitochondrial locations and negatively with cytoskeletal, cytoplasmic, lysosomal and peroxisomal environment. Further analysis demonstrated that subcellular compartment-specific pI distributions are greatly influenced by local pH and organelle membrane charge. Multiple nonlinear regression analysis identified a polynomial function of the two variables that best fitted the mean pI values of the localization-specific pI distributions. A high coefficient of determination calculated for this regression (R2 = 0.98) suggests that local pH and organelle membrane charge are the major factors responsible for variation of the intracellular localization-specific pI profiles. Conclusions Our study demonstrates that strong correlations exist between protein pI and subcellular localization. The specific pI distributions at different subcellular locations are defined by local environment. Predominantly, it is the local pH and membrane charge that shape the organelle-specific protein pI patterns. These findings expand our understanding of spatial organization of the human proteome. Bioinformatics (dpeaa)DE-He213 Human proteome (dpeaa)DE-He213 Protein pI (dpeaa)DE-He213 Protein localization (dpeaa)DE-He213 Regression analysis (dpeaa)DE-He213 Tokmakov, Alexander A. aut Sato, Ken-Ichi aut Stefanov, Vasily E. aut Yamada, Yutaka aut Sakurai, Tetsuya aut Enthalten in BMC cell biology London : BioMed Central, 2000 20(2019), 1 vom: 20. Aug. (DE-627)326644830 (DE-600)2041486-9 1471-2121 nnns volume:20 year:2019 number:1 day:20 month:08 https://dx.doi.org/10.1186/s12860-019-0221-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_22 GBV_ILN_2003 GBV_ILN_2008 GBV_ILN_2021 GBV_ILN_4305 AR 20 2019 1 20 08 |
| allfieldsGer |
10.1186/s12860-019-0221-4 doi (DE-627)SPR026940620 (SPR)s12860-019-0221-4-e DE-627 ger DE-627 rakwb eng Kurotani, Atsushi verfasserin aut Localization-specific distributions of protein pI in human proteome are governed by local pH and membrane charge 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s). 2019 Background Whole-proteome distributions of protein isoelectric point (pI) values in different organisms are bi- or trimodal with some variations. It was suggested that the observed multimodality of the proteome-wide pI distributions is associated with subcellular localization-specific differences in the local pI distributions. However, the factors responsible for variation of the intracellular localization-specific pI profiles have not been investigated in detail. Results In this work, we explored proteome-wide pI distributions of 32,138 human proteins predicted to reside in 10 subcellular compartments, as well as the pI distributions of experimentally observed lysosomal and Golgi proteins. The distributions were found to differ significantly, although all of them adhered to the major recurrent bimodal pattern. Grossly, acid-biased and alkaline-biased patterns with various minor statistical features were observed at different subcellular locations. Bioinformatics analysis revealed the existence of strong statistically significant correlations between protein pI and subcellular localization. Most markedly, protein pI was found to correlate positively with nuclear and mitochondrial locations and negatively with cytoskeletal, cytoplasmic, lysosomal and peroxisomal environment. Further analysis demonstrated that subcellular compartment-specific pI distributions are greatly influenced by local pH and organelle membrane charge. Multiple nonlinear regression analysis identified a polynomial function of the two variables that best fitted the mean pI values of the localization-specific pI distributions. A high coefficient of determination calculated for this regression (R2 = 0.98) suggests that local pH and organelle membrane charge are the major factors responsible for variation of the intracellular localization-specific pI profiles. Conclusions Our study demonstrates that strong correlations exist between protein pI and subcellular localization. The specific pI distributions at different subcellular locations are defined by local environment. Predominantly, it is the local pH and membrane charge that shape the organelle-specific protein pI patterns. These findings expand our understanding of spatial organization of the human proteome. Bioinformatics (dpeaa)DE-He213 Human proteome (dpeaa)DE-He213 Protein pI (dpeaa)DE-He213 Protein localization (dpeaa)DE-He213 Regression analysis (dpeaa)DE-He213 Tokmakov, Alexander A. aut Sato, Ken-Ichi aut Stefanov, Vasily E. aut Yamada, Yutaka aut Sakurai, Tetsuya aut Enthalten in BMC cell biology London : BioMed Central, 2000 20(2019), 1 vom: 20. Aug. (DE-627)326644830 (DE-600)2041486-9 1471-2121 nnns volume:20 year:2019 number:1 day:20 month:08 https://dx.doi.org/10.1186/s12860-019-0221-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_22 GBV_ILN_2003 GBV_ILN_2008 GBV_ILN_2021 GBV_ILN_4305 AR 20 2019 1 20 08 |
| allfieldsSound |
10.1186/s12860-019-0221-4 doi (DE-627)SPR026940620 (SPR)s12860-019-0221-4-e DE-627 ger DE-627 rakwb eng Kurotani, Atsushi verfasserin aut Localization-specific distributions of protein pI in human proteome are governed by local pH and membrane charge 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s). 2019 Background Whole-proteome distributions of protein isoelectric point (pI) values in different organisms are bi- or trimodal with some variations. It was suggested that the observed multimodality of the proteome-wide pI distributions is associated with subcellular localization-specific differences in the local pI distributions. However, the factors responsible for variation of the intracellular localization-specific pI profiles have not been investigated in detail. Results In this work, we explored proteome-wide pI distributions of 32,138 human proteins predicted to reside in 10 subcellular compartments, as well as the pI distributions of experimentally observed lysosomal and Golgi proteins. The distributions were found to differ significantly, although all of them adhered to the major recurrent bimodal pattern. Grossly, acid-biased and alkaline-biased patterns with various minor statistical features were observed at different subcellular locations. Bioinformatics analysis revealed the existence of strong statistically significant correlations between protein pI and subcellular localization. Most markedly, protein pI was found to correlate positively with nuclear and mitochondrial locations and negatively with cytoskeletal, cytoplasmic, lysosomal and peroxisomal environment. Further analysis demonstrated that subcellular compartment-specific pI distributions are greatly influenced by local pH and organelle membrane charge. Multiple nonlinear regression analysis identified a polynomial function of the two variables that best fitted the mean pI values of the localization-specific pI distributions. A high coefficient of determination calculated for this regression (R2 = 0.98) suggests that local pH and organelle membrane charge are the major factors responsible for variation of the intracellular localization-specific pI profiles. Conclusions Our study demonstrates that strong correlations exist between protein pI and subcellular localization. The specific pI distributions at different subcellular locations are defined by local environment. Predominantly, it is the local pH and membrane charge that shape the organelle-specific protein pI patterns. These findings expand our understanding of spatial organization of the human proteome. Bioinformatics (dpeaa)DE-He213 Human proteome (dpeaa)DE-He213 Protein pI (dpeaa)DE-He213 Protein localization (dpeaa)DE-He213 Regression analysis (dpeaa)DE-He213 Tokmakov, Alexander A. aut Sato, Ken-Ichi aut Stefanov, Vasily E. aut Yamada, Yutaka aut Sakurai, Tetsuya aut Enthalten in BMC cell biology London : BioMed Central, 2000 20(2019), 1 vom: 20. Aug. (DE-627)326644830 (DE-600)2041486-9 1471-2121 nnns volume:20 year:2019 number:1 day:20 month:08 https://dx.doi.org/10.1186/s12860-019-0221-4 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_22 GBV_ILN_2003 GBV_ILN_2008 GBV_ILN_2021 GBV_ILN_4305 AR 20 2019 1 20 08 |
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Kurotani, Atsushi @@aut@@ Tokmakov, Alexander A. @@aut@@ Sato, Ken-Ichi @@aut@@ Stefanov, Vasily E. @@aut@@ Yamada, Yutaka @@aut@@ Sakurai, Tetsuya @@aut@@ |
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It was suggested that the observed multimodality of the proteome-wide pI distributions is associated with subcellular localization-specific differences in the local pI distributions. However, the factors responsible for variation of the intracellular localization-specific pI profiles have not been investigated in detail. Results In this work, we explored proteome-wide pI distributions of 32,138 human proteins predicted to reside in 10 subcellular compartments, as well as the pI distributions of experimentally observed lysosomal and Golgi proteins. The distributions were found to differ significantly, although all of them adhered to the major recurrent bimodal pattern. Grossly, acid-biased and alkaline-biased patterns with various minor statistical features were observed at different subcellular locations. Bioinformatics analysis revealed the existence of strong statistically significant correlations between protein pI and subcellular localization. Most markedly, protein pI was found to correlate positively with nuclear and mitochondrial locations and negatively with cytoskeletal, cytoplasmic, lysosomal and peroxisomal environment. Further analysis demonstrated that subcellular compartment-specific pI distributions are greatly influenced by local pH and organelle membrane charge. Multiple nonlinear regression analysis identified a polynomial function of the two variables that best fitted the mean pI values of the localization-specific pI distributions. A high coefficient of determination calculated for this regression (R2 = 0.98) suggests that local pH and organelle membrane charge are the major factors responsible for variation of the intracellular localization-specific pI profiles. Conclusions Our study demonstrates that strong correlations exist between protein pI and subcellular localization. The specific pI distributions at different subcellular locations are defined by local environment. 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Kurotani, Atsushi misc Bioinformatics misc Human proteome misc Protein pI misc Protein localization misc Regression analysis Localization-specific distributions of protein pI in human proteome are governed by local pH and membrane charge |
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Localization-specific distributions of protein pI in human proteome are governed by local pH and membrane charge Bioinformatics (dpeaa)DE-He213 Human proteome (dpeaa)DE-He213 Protein pI (dpeaa)DE-He213 Protein localization (dpeaa)DE-He213 Regression analysis (dpeaa)DE-He213 |
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Kurotani, Atsushi Tokmakov, Alexander A. Sato, Ken-Ichi Stefanov, Vasily E. Yamada, Yutaka Sakurai, Tetsuya |
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localization-specific distributions of protein pi in human proteome are governed by local ph and membrane charge |
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Localization-specific distributions of protein pI in human proteome are governed by local pH and membrane charge |
| abstract |
Background Whole-proteome distributions of protein isoelectric point (pI) values in different organisms are bi- or trimodal with some variations. It was suggested that the observed multimodality of the proteome-wide pI distributions is associated with subcellular localization-specific differences in the local pI distributions. However, the factors responsible for variation of the intracellular localization-specific pI profiles have not been investigated in detail. Results In this work, we explored proteome-wide pI distributions of 32,138 human proteins predicted to reside in 10 subcellular compartments, as well as the pI distributions of experimentally observed lysosomal and Golgi proteins. The distributions were found to differ significantly, although all of them adhered to the major recurrent bimodal pattern. Grossly, acid-biased and alkaline-biased patterns with various minor statistical features were observed at different subcellular locations. Bioinformatics analysis revealed the existence of strong statistically significant correlations between protein pI and subcellular localization. Most markedly, protein pI was found to correlate positively with nuclear and mitochondrial locations and negatively with cytoskeletal, cytoplasmic, lysosomal and peroxisomal environment. Further analysis demonstrated that subcellular compartment-specific pI distributions are greatly influenced by local pH and organelle membrane charge. Multiple nonlinear regression analysis identified a polynomial function of the two variables that best fitted the mean pI values of the localization-specific pI distributions. A high coefficient of determination calculated for this regression (R2 = 0.98) suggests that local pH and organelle membrane charge are the major factors responsible for variation of the intracellular localization-specific pI profiles. Conclusions Our study demonstrates that strong correlations exist between protein pI and subcellular localization. The specific pI distributions at different subcellular locations are defined by local environment. Predominantly, it is the local pH and membrane charge that shape the organelle-specific protein pI patterns. These findings expand our understanding of spatial organization of the human proteome. © The Author(s). 2019 |
| abstractGer |
Background Whole-proteome distributions of protein isoelectric point (pI) values in different organisms are bi- or trimodal with some variations. It was suggested that the observed multimodality of the proteome-wide pI distributions is associated with subcellular localization-specific differences in the local pI distributions. However, the factors responsible for variation of the intracellular localization-specific pI profiles have not been investigated in detail. Results In this work, we explored proteome-wide pI distributions of 32,138 human proteins predicted to reside in 10 subcellular compartments, as well as the pI distributions of experimentally observed lysosomal and Golgi proteins. The distributions were found to differ significantly, although all of them adhered to the major recurrent bimodal pattern. Grossly, acid-biased and alkaline-biased patterns with various minor statistical features were observed at different subcellular locations. Bioinformatics analysis revealed the existence of strong statistically significant correlations between protein pI and subcellular localization. Most markedly, protein pI was found to correlate positively with nuclear and mitochondrial locations and negatively with cytoskeletal, cytoplasmic, lysosomal and peroxisomal environment. Further analysis demonstrated that subcellular compartment-specific pI distributions are greatly influenced by local pH and organelle membrane charge. Multiple nonlinear regression analysis identified a polynomial function of the two variables that best fitted the mean pI values of the localization-specific pI distributions. A high coefficient of determination calculated for this regression (R2 = 0.98) suggests that local pH and organelle membrane charge are the major factors responsible for variation of the intracellular localization-specific pI profiles. Conclusions Our study demonstrates that strong correlations exist between protein pI and subcellular localization. The specific pI distributions at different subcellular locations are defined by local environment. Predominantly, it is the local pH and membrane charge that shape the organelle-specific protein pI patterns. These findings expand our understanding of spatial organization of the human proteome. © The Author(s). 2019 |
| abstract_unstemmed |
Background Whole-proteome distributions of protein isoelectric point (pI) values in different organisms are bi- or trimodal with some variations. It was suggested that the observed multimodality of the proteome-wide pI distributions is associated with subcellular localization-specific differences in the local pI distributions. However, the factors responsible for variation of the intracellular localization-specific pI profiles have not been investigated in detail. Results In this work, we explored proteome-wide pI distributions of 32,138 human proteins predicted to reside in 10 subcellular compartments, as well as the pI distributions of experimentally observed lysosomal and Golgi proteins. The distributions were found to differ significantly, although all of them adhered to the major recurrent bimodal pattern. Grossly, acid-biased and alkaline-biased patterns with various minor statistical features were observed at different subcellular locations. Bioinformatics analysis revealed the existence of strong statistically significant correlations between protein pI and subcellular localization. Most markedly, protein pI was found to correlate positively with nuclear and mitochondrial locations and negatively with cytoskeletal, cytoplasmic, lysosomal and peroxisomal environment. Further analysis demonstrated that subcellular compartment-specific pI distributions are greatly influenced by local pH and organelle membrane charge. Multiple nonlinear regression analysis identified a polynomial function of the two variables that best fitted the mean pI values of the localization-specific pI distributions. A high coefficient of determination calculated for this regression (R2 = 0.98) suggests that local pH and organelle membrane charge are the major factors responsible for variation of the intracellular localization-specific pI profiles. Conclusions Our study demonstrates that strong correlations exist between protein pI and subcellular localization. The specific pI distributions at different subcellular locations are defined by local environment. Predominantly, it is the local pH and membrane charge that shape the organelle-specific protein pI patterns. These findings expand our understanding of spatial organization of the human proteome. © The Author(s). 2019 |
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