The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited

Ribosomal protein bL31 in <i<Escherichia coli</i< was initially detected as a short form (62 amino acids) using Kaltschmidt and Wittmann’s two-dimensional polyacrylamide gel electrophoresis (2D PAGE), but the intact form (70 amino acids) was subsequently identified by means of Wada’s imp...
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Gespeichert in:

Autor*in:	Akira Wada [verfasserIn] Masami Ueta [verfasserIn] Chieko Wada [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	ribosomal protein bL31 ribosome subunit assembly protease 7 RFHR 2D PAGE method translational activity

Übergeordnetes Werk:	In: International Journal of Molecular Sciences - MDPI AG, 2003, 24(2023), 4, p 3445
Übergeordnetes Werk:	volume:24 ; year:2023 ; number:4, p 3445

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc Journal toc

DOI / URN:	10.3390/ijms24043445

Katalog-ID:	DOAJ080261469

Internformat


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520			\|a Ribosomal protein bL31 in <i<Escherichia coli</i< was initially detected as a short form (62 amino acids) using Kaltschmidt and Wittmann’s two-dimensional polyacrylamide gel electrophoresis (2D PAGE), but the intact form (70 amino acids) was subsequently identified by means of Wada’s improved radical-free and highly reducing (RFHR) 2D PAGE, which was consistent with the analysis of its encoding gene <i<rpmE</i<. Ribosomes routinely prepared from the K12 wild-type strain contained both forms of bL31. Δ<i<ompT</i< cells, which lack protease 7, only contained intact bL31, suggesting that protease 7 cleaves intact bL31 and generates short bL31 during ribosome preparation from wild-type cells. Intact bL31 was required for subunit association, and its eight cleaved C-terminal amino acids contributed to this function. 70S ribosomes protected bL31 from cleavage by protease 7, but free 50S did not. In vitro translation was assayed using three systems. The translational activities of wild-type and Δ<i<rpmE</i< ribosomes were 20% and 40% lower than those of Δ<i<ompT</i< ribosomes, which contained one copy of intact bL31. The deletion of bL31 reduces cell growth. A structural analysis predicted that bL31 spans the 30S and 50S subunits, consistent with its functions in 70S association and translation. It is important to re-analyze in vitro translation with ribosomes containing only intact bL31.
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allfields	10.3390/ijms24043445 doi (DE-627)DOAJ080261469 (DE-599)DOAJ6c650a044b214354988f508c8be9eaf1 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Akira Wada verfasserin aut The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ribosomal protein bL31 in <i<Escherichia coli</i< was initially detected as a short form (62 amino acids) using Kaltschmidt and Wittmann’s two-dimensional polyacrylamide gel electrophoresis (2D PAGE), but the intact form (70 amino acids) was subsequently identified by means of Wada’s improved radical-free and highly reducing (RFHR) 2D PAGE, which was consistent with the analysis of its encoding gene <i<rpmE</i<. Ribosomes routinely prepared from the K12 wild-type strain contained both forms of bL31. Δ<i<ompT</i< cells, which lack protease 7, only contained intact bL31, suggesting that protease 7 cleaves intact bL31 and generates short bL31 during ribosome preparation from wild-type cells. Intact bL31 was required for subunit association, and its eight cleaved C-terminal amino acids contributed to this function. 70S ribosomes protected bL31 from cleavage by protease 7, but free 50S did not. In vitro translation was assayed using three systems. The translational activities of wild-type and Δ<i<rpmE</i< ribosomes were 20% and 40% lower than those of Δ<i<ompT</i< ribosomes, which contained one copy of intact bL31. The deletion of bL31 reduces cell growth. A structural analysis predicted that bL31 spans the 30S and 50S subunits, consistent with its functions in 70S association and translation. It is important to re-analyze in vitro translation with ribosomes containing only intact bL31. ribosomal protein bL31 ribosome subunit assembly protease 7 RFHR 2D PAGE method translational activity Biology (General) Chemistry Masami Ueta verfasserin aut Chieko Wada verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 24(2023), 4, p 3445 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:24 year:2023 number:4, p 3445 https://doi.org/10.3390/ijms24043445 kostenfrei https://doaj.org/article/6c650a044b214354988f508c8be9eaf1 kostenfrei https://www.mdpi.com/1422-0067/24/4/3445 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 24 2023 4, p 3445
spelling	10.3390/ijms24043445 doi (DE-627)DOAJ080261469 (DE-599)DOAJ6c650a044b214354988f508c8be9eaf1 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Akira Wada verfasserin aut The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ribosomal protein bL31 in <i<Escherichia coli</i< was initially detected as a short form (62 amino acids) using Kaltschmidt and Wittmann’s two-dimensional polyacrylamide gel electrophoresis (2D PAGE), but the intact form (70 amino acids) was subsequently identified by means of Wada’s improved radical-free and highly reducing (RFHR) 2D PAGE, which was consistent with the analysis of its encoding gene <i<rpmE</i<. Ribosomes routinely prepared from the K12 wild-type strain contained both forms of bL31. Δ<i<ompT</i< cells, which lack protease 7, only contained intact bL31, suggesting that protease 7 cleaves intact bL31 and generates short bL31 during ribosome preparation from wild-type cells. Intact bL31 was required for subunit association, and its eight cleaved C-terminal amino acids contributed to this function. 70S ribosomes protected bL31 from cleavage by protease 7, but free 50S did not. In vitro translation was assayed using three systems. The translational activities of wild-type and Δ<i<rpmE</i< ribosomes were 20% and 40% lower than those of Δ<i<ompT</i< ribosomes, which contained one copy of intact bL31. The deletion of bL31 reduces cell growth. A structural analysis predicted that bL31 spans the 30S and 50S subunits, consistent with its functions in 70S association and translation. It is important to re-analyze in vitro translation with ribosomes containing only intact bL31. ribosomal protein bL31 ribosome subunit assembly protease 7 RFHR 2D PAGE method translational activity Biology (General) Chemistry Masami Ueta verfasserin aut Chieko Wada verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 24(2023), 4, p 3445 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:24 year:2023 number:4, p 3445 https://doi.org/10.3390/ijms24043445 kostenfrei https://doaj.org/article/6c650a044b214354988f508c8be9eaf1 kostenfrei https://www.mdpi.com/1422-0067/24/4/3445 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 24 2023 4, p 3445
allfields_unstemmed	10.3390/ijms24043445 doi (DE-627)DOAJ080261469 (DE-599)DOAJ6c650a044b214354988f508c8be9eaf1 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Akira Wada verfasserin aut The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ribosomal protein bL31 in <i<Escherichia coli</i< was initially detected as a short form (62 amino acids) using Kaltschmidt and Wittmann’s two-dimensional polyacrylamide gel electrophoresis (2D PAGE), but the intact form (70 amino acids) was subsequently identified by means of Wada’s improved radical-free and highly reducing (RFHR) 2D PAGE, which was consistent with the analysis of its encoding gene <i<rpmE</i<. Ribosomes routinely prepared from the K12 wild-type strain contained both forms of bL31. Δ<i<ompT</i< cells, which lack protease 7, only contained intact bL31, suggesting that protease 7 cleaves intact bL31 and generates short bL31 during ribosome preparation from wild-type cells. Intact bL31 was required for subunit association, and its eight cleaved C-terminal amino acids contributed to this function. 70S ribosomes protected bL31 from cleavage by protease 7, but free 50S did not. In vitro translation was assayed using three systems. The translational activities of wild-type and Δ<i<rpmE</i< ribosomes were 20% and 40% lower than those of Δ<i<ompT</i< ribosomes, which contained one copy of intact bL31. The deletion of bL31 reduces cell growth. A structural analysis predicted that bL31 spans the 30S and 50S subunits, consistent with its functions in 70S association and translation. It is important to re-analyze in vitro translation with ribosomes containing only intact bL31. ribosomal protein bL31 ribosome subunit assembly protease 7 RFHR 2D PAGE method translational activity Biology (General) Chemistry Masami Ueta verfasserin aut Chieko Wada verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 24(2023), 4, p 3445 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:24 year:2023 number:4, p 3445 https://doi.org/10.3390/ijms24043445 kostenfrei https://doaj.org/article/6c650a044b214354988f508c8be9eaf1 kostenfrei https://www.mdpi.com/1422-0067/24/4/3445 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 24 2023 4, p 3445
allfieldsGer	10.3390/ijms24043445 doi (DE-627)DOAJ080261469 (DE-599)DOAJ6c650a044b214354988f508c8be9eaf1 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Akira Wada verfasserin aut The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ribosomal protein bL31 in <i<Escherichia coli</i< was initially detected as a short form (62 amino acids) using Kaltschmidt and Wittmann’s two-dimensional polyacrylamide gel electrophoresis (2D PAGE), but the intact form (70 amino acids) was subsequently identified by means of Wada’s improved radical-free and highly reducing (RFHR) 2D PAGE, which was consistent with the analysis of its encoding gene <i<rpmE</i<. Ribosomes routinely prepared from the K12 wild-type strain contained both forms of bL31. Δ<i<ompT</i< cells, which lack protease 7, only contained intact bL31, suggesting that protease 7 cleaves intact bL31 and generates short bL31 during ribosome preparation from wild-type cells. Intact bL31 was required for subunit association, and its eight cleaved C-terminal amino acids contributed to this function. 70S ribosomes protected bL31 from cleavage by protease 7, but free 50S did not. In vitro translation was assayed using three systems. The translational activities of wild-type and Δ<i<rpmE</i< ribosomes were 20% and 40% lower than those of Δ<i<ompT</i< ribosomes, which contained one copy of intact bL31. The deletion of bL31 reduces cell growth. A structural analysis predicted that bL31 spans the 30S and 50S subunits, consistent with its functions in 70S association and translation. It is important to re-analyze in vitro translation with ribosomes containing only intact bL31. ribosomal protein bL31 ribosome subunit assembly protease 7 RFHR 2D PAGE method translational activity Biology (General) Chemistry Masami Ueta verfasserin aut Chieko Wada verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 24(2023), 4, p 3445 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:24 year:2023 number:4, p 3445 https://doi.org/10.3390/ijms24043445 kostenfrei https://doaj.org/article/6c650a044b214354988f508c8be9eaf1 kostenfrei https://www.mdpi.com/1422-0067/24/4/3445 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 24 2023 4, p 3445
allfieldsSound	10.3390/ijms24043445 doi (DE-627)DOAJ080261469 (DE-599)DOAJ6c650a044b214354988f508c8be9eaf1 DE-627 ger DE-627 rakwb eng QH301-705.5 QD1-999 Akira Wada verfasserin aut The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Ribosomal protein bL31 in <i<Escherichia coli</i< was initially detected as a short form (62 amino acids) using Kaltschmidt and Wittmann’s two-dimensional polyacrylamide gel electrophoresis (2D PAGE), but the intact form (70 amino acids) was subsequently identified by means of Wada’s improved radical-free and highly reducing (RFHR) 2D PAGE, which was consistent with the analysis of its encoding gene <i<rpmE</i<. Ribosomes routinely prepared from the K12 wild-type strain contained both forms of bL31. Δ<i<ompT</i< cells, which lack protease 7, only contained intact bL31, suggesting that protease 7 cleaves intact bL31 and generates short bL31 during ribosome preparation from wild-type cells. Intact bL31 was required for subunit association, and its eight cleaved C-terminal amino acids contributed to this function. 70S ribosomes protected bL31 from cleavage by protease 7, but free 50S did not. In vitro translation was assayed using three systems. The translational activities of wild-type and Δ<i<rpmE</i< ribosomes were 20% and 40% lower than those of Δ<i<ompT</i< ribosomes, which contained one copy of intact bL31. The deletion of bL31 reduces cell growth. A structural analysis predicted that bL31 spans the 30S and 50S subunits, consistent with its functions in 70S association and translation. It is important to re-analyze in vitro translation with ribosomes containing only intact bL31. ribosomal protein bL31 ribosome subunit assembly protease 7 RFHR 2D PAGE method translational activity Biology (General) Chemistry Masami Ueta verfasserin aut Chieko Wada verfasserin aut In International Journal of Molecular Sciences MDPI AG, 2003 24(2023), 4, p 3445 (DE-627)316340715 (DE-600)2019364-6 14220067 nnns volume:24 year:2023 number:4, p 3445 https://doi.org/10.3390/ijms24043445 kostenfrei https://doaj.org/article/6c650a044b214354988f508c8be9eaf1 kostenfrei https://www.mdpi.com/1422-0067/24/4/3445 kostenfrei https://doaj.org/toc/1661-6596 Journal toc kostenfrei https://doaj.org/toc/1422-0067 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 24 2023 4, p 3445
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callnumber-first	Q - Science
author	Akira Wada
spellingShingle	Akira Wada misc QH301-705.5 misc QD1-999 misc ribosomal protein bL31 misc ribosome subunit assembly misc protease 7 misc RFHR 2D PAGE method misc translational activity misc Biology (General) misc Chemistry The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited
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topic_title	QH301-705.5 QD1-999 The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited ribosomal protein bL31 ribosome subunit assembly protease 7 RFHR 2D PAGE method translational activity
topic	misc QH301-705.5 misc QD1-999 misc ribosomal protein bL31 misc ribosome subunit assembly misc protease 7 misc RFHR 2D PAGE method misc translational activity misc Biology (General) misc Chemistry
topic_unstemmed	misc QH301-705.5 misc QD1-999 misc ribosomal protein bL31 misc ribosome subunit assembly misc protease 7 misc RFHR 2D PAGE method misc translational activity misc Biology (General) misc Chemistry
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title	The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited
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title_full	The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited
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title_sort	discovery of ribosomal protein bl31 from <i<escherichia coli</i<: a long story revisited
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title_auth	The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited
abstract	Ribosomal protein bL31 in <i<Escherichia coli</i< was initially detected as a short form (62 amino acids) using Kaltschmidt and Wittmann’s two-dimensional polyacrylamide gel electrophoresis (2D PAGE), but the intact form (70 amino acids) was subsequently identified by means of Wada’s improved radical-free and highly reducing (RFHR) 2D PAGE, which was consistent with the analysis of its encoding gene <i<rpmE</i<. Ribosomes routinely prepared from the K12 wild-type strain contained both forms of bL31. Δ<i<ompT</i< cells, which lack protease 7, only contained intact bL31, suggesting that protease 7 cleaves intact bL31 and generates short bL31 during ribosome preparation from wild-type cells. Intact bL31 was required for subunit association, and its eight cleaved C-terminal amino acids contributed to this function. 70S ribosomes protected bL31 from cleavage by protease 7, but free 50S did not. In vitro translation was assayed using three systems. The translational activities of wild-type and Δ<i<rpmE</i< ribosomes were 20% and 40% lower than those of Δ<i<ompT</i< ribosomes, which contained one copy of intact bL31. The deletion of bL31 reduces cell growth. A structural analysis predicted that bL31 spans the 30S and 50S subunits, consistent with its functions in 70S association and translation. It is important to re-analyze in vitro translation with ribosomes containing only intact bL31.
abstractGer	Ribosomal protein bL31 in <i<Escherichia coli</i< was initially detected as a short form (62 amino acids) using Kaltschmidt and Wittmann’s two-dimensional polyacrylamide gel electrophoresis (2D PAGE), but the intact form (70 amino acids) was subsequently identified by means of Wada’s improved radical-free and highly reducing (RFHR) 2D PAGE, which was consistent with the analysis of its encoding gene <i<rpmE</i<. Ribosomes routinely prepared from the K12 wild-type strain contained both forms of bL31. Δ<i<ompT</i< cells, which lack protease 7, only contained intact bL31, suggesting that protease 7 cleaves intact bL31 and generates short bL31 during ribosome preparation from wild-type cells. Intact bL31 was required for subunit association, and its eight cleaved C-terminal amino acids contributed to this function. 70S ribosomes protected bL31 from cleavage by protease 7, but free 50S did not. In vitro translation was assayed using three systems. The translational activities of wild-type and Δ<i<rpmE</i< ribosomes were 20% and 40% lower than those of Δ<i<ompT</i< ribosomes, which contained one copy of intact bL31. The deletion of bL31 reduces cell growth. A structural analysis predicted that bL31 spans the 30S and 50S subunits, consistent with its functions in 70S association and translation. It is important to re-analyze in vitro translation with ribosomes containing only intact bL31.
abstract_unstemmed	Ribosomal protein bL31 in <i<Escherichia coli</i< was initially detected as a short form (62 amino acids) using Kaltschmidt and Wittmann’s two-dimensional polyacrylamide gel electrophoresis (2D PAGE), but the intact form (70 amino acids) was subsequently identified by means of Wada’s improved radical-free and highly reducing (RFHR) 2D PAGE, which was consistent with the analysis of its encoding gene <i<rpmE</i<. Ribosomes routinely prepared from the K12 wild-type strain contained both forms of bL31. Δ<i<ompT</i< cells, which lack protease 7, only contained intact bL31, suggesting that protease 7 cleaves intact bL31 and generates short bL31 during ribosome preparation from wild-type cells. Intact bL31 was required for subunit association, and its eight cleaved C-terminal amino acids contributed to this function. 70S ribosomes protected bL31 from cleavage by protease 7, but free 50S did not. In vitro translation was assayed using three systems. The translational activities of wild-type and Δ<i<rpmE</i< ribosomes were 20% and 40% lower than those of Δ<i<ompT</i< ribosomes, which contained one copy of intact bL31. The deletion of bL31 reduces cell growth. A structural analysis predicted that bL31 spans the 30S and 50S subunits, consistent with its functions in 70S association and translation. It is important to re-analyze in vitro translation with ribosomes containing only intact bL31.
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container_issue	4, p 3445
title_short	The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited
url	https://doi.org/10.3390/ijms24043445 https://doaj.org/article/6c650a044b214354988f508c8be9eaf1 https://www.mdpi.com/1422-0067/24/4/3445 https://doaj.org/toc/1661-6596 https://doaj.org/toc/1422-0067
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Ribosomes routinely prepared from the K12 wild-type strain contained both forms of bL31. Δ<i<ompT</i< cells, which lack protease 7, only contained intact bL31, suggesting that protease 7 cleaves intact bL31 and generates short bL31 during ribosome preparation from wild-type cells. Intact bL31 was required for subunit association, and its eight cleaved C-terminal amino acids contributed to this function. 70S ribosomes protected bL31 from cleavage by protease 7, but free 50S did not. In vitro translation was assayed using three systems. The translational activities of wild-type and Δ<i<rpmE</i< ribosomes were 20% and 40% lower than those of Δ<i<ompT</i< ribosomes, which contained one copy of intact bL31. The deletion of bL31 reduces cell growth. A structural analysis predicted that bL31 spans the 30S and 50S subunits, consistent with its functions in 70S association and translation. 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The Discovery of Ribosomal Protein bL31 from <i<Escherichia coli</i<: A Long Story Revisited

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