Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport
The segregation of approximately two dozen distinct mRNAs from yeast mother to daughter cell cytoplasm is a classical paradigm for eukaryotic mRNA transport. The information for transport resides in an mRNA element 40-100 nt in length, known as "zipcode." Targeted transport requires proper...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Nimisha Singh [verfasserIn] |
|---|
| Format: |
Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences |
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| Schlagwörter: |
Saccharomyces cerevisiae Proteins - chemistry RNA-Binding Proteins - metabolism RNA-Binding Proteins - chemistry |
|---|
| Übergeordnetes Werk: |
Enthalten in: Proceedings of the National Academy of Sciences of the United States of America - Washington, DC : NAS, 1877, 112(2015), 1, Seite 142-147 |
|---|---|
| Übergeordnetes Werk: |
volume:112 ; year:2015 ; number:1 ; pages:142-147 |
| Links: |
|---|
| DOI / URN: |
10.1073/pnas.1423194112 |
|---|
| Katalog-ID: |
OLC1961710323 |
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| 520 | |a The segregation of approximately two dozen distinct mRNAs from yeast mother to daughter cell cytoplasm is a classical paradigm for eukaryotic mRNA transport. The information for transport resides in an mRNA element 40-100 nt in length, known as "zipcode." Targeted transport requires properly positioned actin filaments and cooperative loading of mRNA cargo to myosin. Cargo loading to myosin uses myosin 4 protein (Myo4p), swi5p-dependent HO expression 2 protein (She2p) and 3 protein (She3p), and zipcode. We previously determined a crystal structure of Myo4p and She3p, their 1:2 stoichiometry and interactome; we furthermore showed that the motor complex assembly requires two Myo4p⋅She3p heterotrimers, one She2p tetramer, and at least a single zipcode to yield a stable complex of [Myo4p⋅She3p⋅She2p⋅zipcode] in 2:4:4:1 stoichiometry in vitro. Here, we report a structure at 2.8-Å resolution of a cocrystal of a She2p tetramer bound to a segment of She3p. In this crystal structure, the She3p segment forms a striking hook that binds to a shallow hydrophobic pocket on the surface of each She2p subunit of the tetramer. Both She3p hook and cognate She2p binding pocket are composed of highly conserved residues. We also discovered a highly conserved region of She3p upstream of its hook region. Because this region consists of basic and aromatic residues, it likely represents part of She3p's binding activity for zipcode. Because She2p also exhibits zipcode-binding activity, we suggest that "hooking" She3p onto She2p aligns each of their zipcode-binding activities into a high-affinity site, thereby linking motor assembly to zipcode. | ||
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| 650 | 4 | |a Amino Acids - metabolism | |
| 650 | 4 | |a Myosins - metabolism | |
| 650 | 4 | |a Cytoplasm - metabolism | |
| 650 | 4 | |a RNA, Messenger - metabolism | |
| 650 | 4 | |a Saccharomyces cerevisiae Proteins - chemistry | |
| 650 | 4 | |a Peptides - chemistry | |
| 650 | 4 | |a RNA, Messenger - genetics | |
| 650 | 4 | |a RNA-Binding Proteins - metabolism | |
| 650 | 4 | |a Peptides - metabolism | |
| 650 | 4 | |a RNA-Binding Proteins - chemistry | |
| 650 | 4 | |a Saccharomyces cerevisiae Proteins - metabolism | |
| 650 | 4 | |a Biological transport, Active | |
| 650 | 4 | |a Observations | |
| 650 | 4 | |a Messenger RNA | |
| 650 | 4 | |a Cytoplasm | |
| 650 | 4 | |a Genetic aspects | |
| 650 | 4 | |a Physiological aspects | |
| 650 | 4 | |a RNA-protein interactions | |
| 650 | 4 | |a Hydrophobic surfaces | |
| 650 | 4 | |a Binding sites | |
| 650 | 4 | |a Crystal structure | |
| 650 | 4 | |a Crystallography | |
| 650 | 4 | |a Yeast | |
| 700 | 0 | |a Günter Blobel |4 oth | |
| 700 | 0 | |a Hang Shi |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |t Proceedings of the National Academy of Sciences of the United States of America |d Washington, DC : NAS, 1877 |g 112(2015), 1, Seite 142-147 |w (DE-627)129505269 |w (DE-600)209104-5 |w (DE-576)014909189 |x 0027-8424 |7 nnns |
| 773 | 1 | 8 | |g volume:112 |g year:2015 |g number:1 |g pages:142-147 |
| 856 | 4 | 1 | |u http://dx.doi.org/10.1073/pnas.1423194112 |3 Volltext |
| 856 | 4 | 2 | |u http://www.pnas.org/content/112/1/142.abstract |
| 856 | 4 | 2 | |u http://www.ncbi.nlm.nih.gov/pubmed/25535369 |
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10.1073/pnas.1423194112 doi PQ20160617 (DE-627)OLC1961710323 (DE-599)GBVOLC1961710323 (PRQ)c2193-2bbc1b90d405ed37a711e446438a0b634d68cd24570991064f2fc309146e08d3 (KEY)0583363920150000112000100142hookingshe3pontoshe2pformyosinmediatedcytoplasmicm DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Nimisha Singh verfasserin aut Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The segregation of approximately two dozen distinct mRNAs from yeast mother to daughter cell cytoplasm is a classical paradigm for eukaryotic mRNA transport. The information for transport resides in an mRNA element 40-100 nt in length, known as "zipcode." Targeted transport requires properly positioned actin filaments and cooperative loading of mRNA cargo to myosin. Cargo loading to myosin uses myosin 4 protein (Myo4p), swi5p-dependent HO expression 2 protein (She2p) and 3 protein (She3p), and zipcode. We previously determined a crystal structure of Myo4p and She3p, their 1:2 stoichiometry and interactome; we furthermore showed that the motor complex assembly requires two Myo4p⋅She3p heterotrimers, one She2p tetramer, and at least a single zipcode to yield a stable complex of [Myo4p⋅She3p⋅She2p⋅zipcode] in 2:4:4:1 stoichiometry in vitro. Here, we report a structure at 2.8-Å resolution of a cocrystal of a She2p tetramer bound to a segment of She3p. In this crystal structure, the She3p segment forms a striking hook that binds to a shallow hydrophobic pocket on the surface of each She2p subunit of the tetramer. Both She3p hook and cognate She2p binding pocket are composed of highly conserved residues. We also discovered a highly conserved region of She3p upstream of its hook region. Because this region consists of basic and aromatic residues, it likely represents part of She3p's binding activity for zipcode. Because She2p also exhibits zipcode-binding activity, we suggest that "hooking" She3p onto She2p aligns each of their zipcode-binding activities into a high-affinity site, thereby linking motor assembly to zipcode. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Amino Acids - metabolism Myosins - metabolism Cytoplasm - metabolism RNA, Messenger - metabolism Saccharomyces cerevisiae Proteins - chemistry Peptides - chemistry RNA, Messenger - genetics RNA-Binding Proteins - metabolism Peptides - metabolism RNA-Binding Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Biological transport, Active Observations Messenger RNA Cytoplasm Genetic aspects Physiological aspects RNA-protein interactions Hydrophobic surfaces Binding sites Crystal structure Crystallography Yeast Günter Blobel oth Hang Shi oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 1, Seite 142-147 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:1 pages:142-147 http://dx.doi.org/10.1073/pnas.1423194112 Volltext http://www.pnas.org/content/112/1/142.abstract http://www.ncbi.nlm.nih.gov/pubmed/25535369 http://search.proquest.com/docview/1645384934 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 1 142-147 |
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10.1073/pnas.1423194112 doi PQ20160617 (DE-627)OLC1961710323 (DE-599)GBVOLC1961710323 (PRQ)c2193-2bbc1b90d405ed37a711e446438a0b634d68cd24570991064f2fc309146e08d3 (KEY)0583363920150000112000100142hookingshe3pontoshe2pformyosinmediatedcytoplasmicm DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Nimisha Singh verfasserin aut Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The segregation of approximately two dozen distinct mRNAs from yeast mother to daughter cell cytoplasm is a classical paradigm for eukaryotic mRNA transport. The information for transport resides in an mRNA element 40-100 nt in length, known as "zipcode." Targeted transport requires properly positioned actin filaments and cooperative loading of mRNA cargo to myosin. Cargo loading to myosin uses myosin 4 protein (Myo4p), swi5p-dependent HO expression 2 protein (She2p) and 3 protein (She3p), and zipcode. We previously determined a crystal structure of Myo4p and She3p, their 1:2 stoichiometry and interactome; we furthermore showed that the motor complex assembly requires two Myo4p⋅She3p heterotrimers, one She2p tetramer, and at least a single zipcode to yield a stable complex of [Myo4p⋅She3p⋅She2p⋅zipcode] in 2:4:4:1 stoichiometry in vitro. Here, we report a structure at 2.8-Å resolution of a cocrystal of a She2p tetramer bound to a segment of She3p. In this crystal structure, the She3p segment forms a striking hook that binds to a shallow hydrophobic pocket on the surface of each She2p subunit of the tetramer. Both She3p hook and cognate She2p binding pocket are composed of highly conserved residues. We also discovered a highly conserved region of She3p upstream of its hook region. Because this region consists of basic and aromatic residues, it likely represents part of She3p's binding activity for zipcode. Because She2p also exhibits zipcode-binding activity, we suggest that "hooking" She3p onto She2p aligns each of their zipcode-binding activities into a high-affinity site, thereby linking motor assembly to zipcode. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Amino Acids - metabolism Myosins - metabolism Cytoplasm - metabolism RNA, Messenger - metabolism Saccharomyces cerevisiae Proteins - chemistry Peptides - chemistry RNA, Messenger - genetics RNA-Binding Proteins - metabolism Peptides - metabolism RNA-Binding Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Biological transport, Active Observations Messenger RNA Cytoplasm Genetic aspects Physiological aspects RNA-protein interactions Hydrophobic surfaces Binding sites Crystal structure Crystallography Yeast Günter Blobel oth Hang Shi oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 1, Seite 142-147 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:1 pages:142-147 http://dx.doi.org/10.1073/pnas.1423194112 Volltext http://www.pnas.org/content/112/1/142.abstract http://www.ncbi.nlm.nih.gov/pubmed/25535369 http://search.proquest.com/docview/1645384934 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 1 142-147 |
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10.1073/pnas.1423194112 doi PQ20160617 (DE-627)OLC1961710323 (DE-599)GBVOLC1961710323 (PRQ)c2193-2bbc1b90d405ed37a711e446438a0b634d68cd24570991064f2fc309146e08d3 (KEY)0583363920150000112000100142hookingshe3pontoshe2pformyosinmediatedcytoplasmicm DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Nimisha Singh verfasserin aut Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The segregation of approximately two dozen distinct mRNAs from yeast mother to daughter cell cytoplasm is a classical paradigm for eukaryotic mRNA transport. The information for transport resides in an mRNA element 40-100 nt in length, known as "zipcode." Targeted transport requires properly positioned actin filaments and cooperative loading of mRNA cargo to myosin. Cargo loading to myosin uses myosin 4 protein (Myo4p), swi5p-dependent HO expression 2 protein (She2p) and 3 protein (She3p), and zipcode. We previously determined a crystal structure of Myo4p and She3p, their 1:2 stoichiometry and interactome; we furthermore showed that the motor complex assembly requires two Myo4p⋅She3p heterotrimers, one She2p tetramer, and at least a single zipcode to yield a stable complex of [Myo4p⋅She3p⋅She2p⋅zipcode] in 2:4:4:1 stoichiometry in vitro. Here, we report a structure at 2.8-Å resolution of a cocrystal of a She2p tetramer bound to a segment of She3p. In this crystal structure, the She3p segment forms a striking hook that binds to a shallow hydrophobic pocket on the surface of each She2p subunit of the tetramer. Both She3p hook and cognate She2p binding pocket are composed of highly conserved residues. We also discovered a highly conserved region of She3p upstream of its hook region. Because this region consists of basic and aromatic residues, it likely represents part of She3p's binding activity for zipcode. Because She2p also exhibits zipcode-binding activity, we suggest that "hooking" She3p onto She2p aligns each of their zipcode-binding activities into a high-affinity site, thereby linking motor assembly to zipcode. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Amino Acids - metabolism Myosins - metabolism Cytoplasm - metabolism RNA, Messenger - metabolism Saccharomyces cerevisiae Proteins - chemistry Peptides - chemistry RNA, Messenger - genetics RNA-Binding Proteins - metabolism Peptides - metabolism RNA-Binding Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Biological transport, Active Observations Messenger RNA Cytoplasm Genetic aspects Physiological aspects RNA-protein interactions Hydrophobic surfaces Binding sites Crystal structure Crystallography Yeast Günter Blobel oth Hang Shi oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 1, Seite 142-147 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:1 pages:142-147 http://dx.doi.org/10.1073/pnas.1423194112 Volltext http://www.pnas.org/content/112/1/142.abstract http://www.ncbi.nlm.nih.gov/pubmed/25535369 http://search.proquest.com/docview/1645384934 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 1 142-147 |
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10.1073/pnas.1423194112 doi PQ20160617 (DE-627)OLC1961710323 (DE-599)GBVOLC1961710323 (PRQ)c2193-2bbc1b90d405ed37a711e446438a0b634d68cd24570991064f2fc309146e08d3 (KEY)0583363920150000112000100142hookingshe3pontoshe2pformyosinmediatedcytoplasmicm DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Nimisha Singh verfasserin aut Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The segregation of approximately two dozen distinct mRNAs from yeast mother to daughter cell cytoplasm is a classical paradigm for eukaryotic mRNA transport. The information for transport resides in an mRNA element 40-100 nt in length, known as "zipcode." Targeted transport requires properly positioned actin filaments and cooperative loading of mRNA cargo to myosin. Cargo loading to myosin uses myosin 4 protein (Myo4p), swi5p-dependent HO expression 2 protein (She2p) and 3 protein (She3p), and zipcode. We previously determined a crystal structure of Myo4p and She3p, their 1:2 stoichiometry and interactome; we furthermore showed that the motor complex assembly requires two Myo4p⋅She3p heterotrimers, one She2p tetramer, and at least a single zipcode to yield a stable complex of [Myo4p⋅She3p⋅She2p⋅zipcode] in 2:4:4:1 stoichiometry in vitro. Here, we report a structure at 2.8-Å resolution of a cocrystal of a She2p tetramer bound to a segment of She3p. In this crystal structure, the She3p segment forms a striking hook that binds to a shallow hydrophobic pocket on the surface of each She2p subunit of the tetramer. Both She3p hook and cognate She2p binding pocket are composed of highly conserved residues. We also discovered a highly conserved region of She3p upstream of its hook region. Because this region consists of basic and aromatic residues, it likely represents part of She3p's binding activity for zipcode. Because She2p also exhibits zipcode-binding activity, we suggest that "hooking" She3p onto She2p aligns each of their zipcode-binding activities into a high-affinity site, thereby linking motor assembly to zipcode. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Amino Acids - metabolism Myosins - metabolism Cytoplasm - metabolism RNA, Messenger - metabolism Saccharomyces cerevisiae Proteins - chemistry Peptides - chemistry RNA, Messenger - genetics RNA-Binding Proteins - metabolism Peptides - metabolism RNA-Binding Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Biological transport, Active Observations Messenger RNA Cytoplasm Genetic aspects Physiological aspects RNA-protein interactions Hydrophobic surfaces Binding sites Crystal structure Crystallography Yeast Günter Blobel oth Hang Shi oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 1, Seite 142-147 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:1 pages:142-147 http://dx.doi.org/10.1073/pnas.1423194112 Volltext http://www.pnas.org/content/112/1/142.abstract http://www.ncbi.nlm.nih.gov/pubmed/25535369 http://search.proquest.com/docview/1645384934 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 1 142-147 |
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10.1073/pnas.1423194112 doi PQ20160617 (DE-627)OLC1961710323 (DE-599)GBVOLC1961710323 (PRQ)c2193-2bbc1b90d405ed37a711e446438a0b634d68cd24570991064f2fc309146e08d3 (KEY)0583363920150000112000100142hookingshe3pontoshe2pformyosinmediatedcytoplasmicm DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Nimisha Singh verfasserin aut Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The segregation of approximately two dozen distinct mRNAs from yeast mother to daughter cell cytoplasm is a classical paradigm for eukaryotic mRNA transport. The information for transport resides in an mRNA element 40-100 nt in length, known as "zipcode." Targeted transport requires properly positioned actin filaments and cooperative loading of mRNA cargo to myosin. Cargo loading to myosin uses myosin 4 protein (Myo4p), swi5p-dependent HO expression 2 protein (She2p) and 3 protein (She3p), and zipcode. We previously determined a crystal structure of Myo4p and She3p, their 1:2 stoichiometry and interactome; we furthermore showed that the motor complex assembly requires two Myo4p⋅She3p heterotrimers, one She2p tetramer, and at least a single zipcode to yield a stable complex of [Myo4p⋅She3p⋅She2p⋅zipcode] in 2:4:4:1 stoichiometry in vitro. Here, we report a structure at 2.8-Å resolution of a cocrystal of a She2p tetramer bound to a segment of She3p. In this crystal structure, the She3p segment forms a striking hook that binds to a shallow hydrophobic pocket on the surface of each She2p subunit of the tetramer. Both She3p hook and cognate She2p binding pocket are composed of highly conserved residues. We also discovered a highly conserved region of She3p upstream of its hook region. Because this region consists of basic and aromatic residues, it likely represents part of She3p's binding activity for zipcode. Because She2p also exhibits zipcode-binding activity, we suggest that "hooking" She3p onto She2p aligns each of their zipcode-binding activities into a high-affinity site, thereby linking motor assembly to zipcode. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Amino Acids - metabolism Myosins - metabolism Cytoplasm - metabolism RNA, Messenger - metabolism Saccharomyces cerevisiae Proteins - chemistry Peptides - chemistry RNA, Messenger - genetics RNA-Binding Proteins - metabolism Peptides - metabolism RNA-Binding Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Biological transport, Active Observations Messenger RNA Cytoplasm Genetic aspects Physiological aspects RNA-protein interactions Hydrophobic surfaces Binding sites Crystal structure Crystallography Yeast Günter Blobel oth Hang Shi oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 1, Seite 142-147 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:1 pages:142-147 http://dx.doi.org/10.1073/pnas.1423194112 Volltext http://www.pnas.org/content/112/1/142.abstract http://www.ncbi.nlm.nih.gov/pubmed/25535369 http://search.proquest.com/docview/1645384934 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 1 142-147 |
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Hooking She3p onto She2p for myosin-mediated cytoplasmic mRNA transport |
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The segregation of approximately two dozen distinct mRNAs from yeast mother to daughter cell cytoplasm is a classical paradigm for eukaryotic mRNA transport. The information for transport resides in an mRNA element 40-100 nt in length, known as "zipcode." Targeted transport requires properly positioned actin filaments and cooperative loading of mRNA cargo to myosin. Cargo loading to myosin uses myosin 4 protein (Myo4p), swi5p-dependent HO expression 2 protein (She2p) and 3 protein (She3p), and zipcode. We previously determined a crystal structure of Myo4p and She3p, their 1:2 stoichiometry and interactome; we furthermore showed that the motor complex assembly requires two Myo4p⋅She3p heterotrimers, one She2p tetramer, and at least a single zipcode to yield a stable complex of [Myo4p⋅She3p⋅She2p⋅zipcode] in 2:4:4:1 stoichiometry in vitro. Here, we report a structure at 2.8-Å resolution of a cocrystal of a She2p tetramer bound to a segment of She3p. In this crystal structure, the She3p segment forms a striking hook that binds to a shallow hydrophobic pocket on the surface of each She2p subunit of the tetramer. Both She3p hook and cognate She2p binding pocket are composed of highly conserved residues. We also discovered a highly conserved region of She3p upstream of its hook region. Because this region consists of basic and aromatic residues, it likely represents part of She3p's binding activity for zipcode. Because She2p also exhibits zipcode-binding activity, we suggest that "hooking" She3p onto She2p aligns each of their zipcode-binding activities into a high-affinity site, thereby linking motor assembly to zipcode. |
| abstractGer |
The segregation of approximately two dozen distinct mRNAs from yeast mother to daughter cell cytoplasm is a classical paradigm for eukaryotic mRNA transport. The information for transport resides in an mRNA element 40-100 nt in length, known as "zipcode." Targeted transport requires properly positioned actin filaments and cooperative loading of mRNA cargo to myosin. Cargo loading to myosin uses myosin 4 protein (Myo4p), swi5p-dependent HO expression 2 protein (She2p) and 3 protein (She3p), and zipcode. We previously determined a crystal structure of Myo4p and She3p, their 1:2 stoichiometry and interactome; we furthermore showed that the motor complex assembly requires two Myo4p⋅She3p heterotrimers, one She2p tetramer, and at least a single zipcode to yield a stable complex of [Myo4p⋅She3p⋅She2p⋅zipcode] in 2:4:4:1 stoichiometry in vitro. Here, we report a structure at 2.8-Å resolution of a cocrystal of a She2p tetramer bound to a segment of She3p. In this crystal structure, the She3p segment forms a striking hook that binds to a shallow hydrophobic pocket on the surface of each She2p subunit of the tetramer. Both She3p hook and cognate She2p binding pocket are composed of highly conserved residues. We also discovered a highly conserved region of She3p upstream of its hook region. Because this region consists of basic and aromatic residues, it likely represents part of She3p's binding activity for zipcode. Because She2p also exhibits zipcode-binding activity, we suggest that "hooking" She3p onto She2p aligns each of their zipcode-binding activities into a high-affinity site, thereby linking motor assembly to zipcode. |
| abstract_unstemmed |
The segregation of approximately two dozen distinct mRNAs from yeast mother to daughter cell cytoplasm is a classical paradigm for eukaryotic mRNA transport. The information for transport resides in an mRNA element 40-100 nt in length, known as "zipcode." Targeted transport requires properly positioned actin filaments and cooperative loading of mRNA cargo to myosin. Cargo loading to myosin uses myosin 4 protein (Myo4p), swi5p-dependent HO expression 2 protein (She2p) and 3 protein (She3p), and zipcode. We previously determined a crystal structure of Myo4p and She3p, their 1:2 stoichiometry and interactome; we furthermore showed that the motor complex assembly requires two Myo4p⋅She3p heterotrimers, one She2p tetramer, and at least a single zipcode to yield a stable complex of [Myo4p⋅She3p⋅She2p⋅zipcode] in 2:4:4:1 stoichiometry in vitro. Here, we report a structure at 2.8-Å resolution of a cocrystal of a She2p tetramer bound to a segment of She3p. In this crystal structure, the She3p segment forms a striking hook that binds to a shallow hydrophobic pocket on the surface of each She2p subunit of the tetramer. Both She3p hook and cognate She2p binding pocket are composed of highly conserved residues. We also discovered a highly conserved region of She3p upstream of its hook region. Because this region consists of basic and aromatic residues, it likely represents part of She3p's binding activity for zipcode. Because She2p also exhibits zipcode-binding activity, we suggest that "hooking" She3p onto She2p aligns each of their zipcode-binding activities into a high-affinity site, thereby linking motor assembly to zipcode. |
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The information for transport resides in an mRNA element 40-100 nt in length, known as "zipcode." Targeted transport requires properly positioned actin filaments and cooperative loading of mRNA cargo to myosin. Cargo loading to myosin uses myosin 4 protein (Myo4p), swi5p-dependent HO expression 2 protein (She2p) and 3 protein (She3p), and zipcode. We previously determined a crystal structure of Myo4p and She3p, their 1:2 stoichiometry and interactome; we furthermore showed that the motor complex assembly requires two Myo4p⋅She3p heterotrimers, one She2p tetramer, and at least a single zipcode to yield a stable complex of [Myo4p⋅She3p⋅She2p⋅zipcode] in 2:4:4:1 stoichiometry in vitro. Here, we report a structure at 2.8-Å resolution of a cocrystal of a She2p tetramer bound to a segment of She3p. In this crystal structure, the She3p segment forms a striking hook that binds to a shallow hydrophobic pocket on the surface of each She2p subunit of the tetramer. Both She3p hook and cognate She2p binding pocket are composed of highly conserved residues. We also discovered a highly conserved region of She3p upstream of its hook region. Because this region consists of basic and aromatic residues, it likely represents part of She3p's binding activity for zipcode. Because She2p also exhibits zipcode-binding activity, we suggest that "hooking" She3p onto She2p aligns each of their zipcode-binding activities into a high-affinity site, thereby linking motor assembly to zipcode.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Amino Acids - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Myosins - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cytoplasm - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">RNA, Messenger - metabolism</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Saccharomyces cerevisiae Proteins - chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Peptides - chemistry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">RNA, Messenger - 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