The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1
J-proteins are obligate partners of Hsp70s, forming a ubiquitous class of molecular chaperone machinery. The ribosome-associated Hsp70 of yeast Ssb binds nascent polypeptides as they exit the ribosome. Here we report that the ribosome-associated J-protein Zuo1 is the partner of Ssb. However, Zuo1 ef...
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| Veröffentlicht in: | Nature structural & molecular biology 2005-06, Vol.12 (6), p.497-504 |
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| creator | Craig, Elizabeth A Huang, Peggy Gautschi, Matthias Walter, William Rospert, Sabine |
| description | J-proteins are obligate partners of Hsp70s, forming a ubiquitous class of molecular chaperone machinery. The ribosome-associated Hsp70 of yeast Ssb binds nascent polypeptides as they exit the ribosome. Here we report that the ribosome-associated J-protein Zuo1 is the partner of Ssb. However, Zuo1 efficiently stimulates the ATPase activity of Ssb only when in complex with another Hsp70, Ssz1. Ssz1 binds ATP, but none of the 11 different amino acid substitutions in the ATP-binding cleft affected Ssz1 function
in vivo
, suggesting that neither nucleotide binding nor hydrolysis is required. We propose that Ssz1's predominant function in the cell is to facilitate Zuo1's ability to function as a J-protein partner of Ssb on the ribosome, serving as an example of an Hsp70 family member that has evolved to carry out functions distinct from that of a chaperone. |
| doi_str_mv | 10.1038/nsmb942 |
| format | Article |
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in vivo
, suggesting that neither nucleotide binding nor hydrolysis is required. We propose that Ssz1's predominant function in the cell is to facilitate Zuo1's ability to function as a J-protein partner of Ssb on the ribosome, serving as an example of an Hsp70 family member that has evolved to carry out functions distinct from that of a chaperone.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb942</identifier><identifier>PMID: 15908962</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Adenosine Triphosphatases - metabolism ; Adenosine Triphosphate - metabolism ; Amino acids ; ATP ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; DNA binding proteins ; DNA-Binding Proteins - physiology ; HSP70 Heat-Shock Proteins - chemistry ; HSP70 Heat-Shock Proteins - genetics ; HSP70 Heat-Shock Proteins - metabolism ; HSP70 Heat-Shock Proteins - physiology ; Hydrolysis ; Kinetics ; Life Sciences ; Membrane Biology ; Models, Molecular ; Molecular Chaperones ; Phenotype ; Physiological aspects ; Polypeptides ; Protein Conformation ; Protein Structure ; Proteins ; Ribonucleic acid ; Ribosomes ; Ribosomes - metabolism ; RNA ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Saccharomyces cerevisiae Proteins - physiology ; Structure ; Yeast ; Yeasts</subject><ispartof>Nature structural & molecular biology, 2005-06, Vol.12 (6), p.497-504</ispartof><rights>Springer Nature America, Inc. 2005</rights><rights>COPYRIGHT 2005 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jun 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-27afdd7bc816cfec85d787bc4fd0575cb236485b47e5136a6f8b2d8e906183dc3</citedby><cites>FETCH-LOGICAL-c520t-27afdd7bc816cfec85d787bc4fd0575cb236485b47e5136a6f8b2d8e906183dc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15908962$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Craig, Elizabeth A</creatorcontrib><creatorcontrib>Huang, Peggy</creatorcontrib><creatorcontrib>Gautschi, Matthias</creatorcontrib><creatorcontrib>Walter, William</creatorcontrib><creatorcontrib>Rospert, Sabine</creatorcontrib><title>The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>J-proteins are obligate partners of Hsp70s, forming a ubiquitous class of molecular chaperone machinery. The ribosome-associated Hsp70 of yeast Ssb binds nascent polypeptides as they exit the ribosome. Here we report that the ribosome-associated J-protein Zuo1 is the partner of Ssb. However, Zuo1 efficiently stimulates the ATPase activity of Ssb only when in complex with another Hsp70, Ssz1. Ssz1 binds ATP, but none of the 11 different amino acid substitutions in the ATP-binding cleft affected Ssz1 function
in vivo
, suggesting that neither nucleotide binding nor hydrolysis is required. We propose that Ssz1's predominant function in the cell is to facilitate Zuo1's ability to function as a J-protein partner of Ssb on the ribosome, serving as an example of an Hsp70 family member that has evolved to carry out functions distinct from that of a chaperone.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino acids</subject><subject>ATP</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>DNA binding proteins</subject><subject>DNA-Binding Proteins - physiology</subject><subject>HSP70 Heat-Shock Proteins - chemistry</subject><subject>HSP70 Heat-Shock Proteins - genetics</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>HSP70 Heat-Shock Proteins - physiology</subject><subject>Hydrolysis</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Molecular Chaperones</subject><subject>Phenotype</subject><subject>Physiological aspects</subject><subject>Polypeptides</subject><subject>Protein Conformation</subject><subject>Protein Structure</subject><subject>Proteins</subject><subject>Ribonucleic acid</subject><subject>Ribosomes</subject><subject>Ribosomes - metabolism</subject><subject>RNA</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - physiology</subject><subject>Structure</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>1545-9993</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqN0ltrFTEQAOAgiq1V_AXKouDlYWuS3WySx1LUVgoFW198Cdlkctyym5wmWbD99abuseWooOQhl_lmwsAg9JTgfYIb8c6nqZctvYd2CWtZLaVg92_PstlBj1K6wJgyxpuHaIcwiYXs6C46Pf8G1VFac1ydpWtSTcHOo86QqlwCbvYmD8FXwf28x6EPKUxQ65SCGYqz1ad6HUOGwVdf50AeowdOjwmebPY99OXD-_PDo_rk9OPx4cFJbRjFuaZcO2t5bwTpjAMjmOWiXFtnMePM9LTpWsH6lgMjTac7J3pqBUjcEdFY0-yhV0vd8vnlDCmraUgGxlF7CHNSHZcYcyz-CQlvJWn-C2LREtkW-OI3eBHm6Eu3ilJBOeGUF_RyQSs9ghq8Czlqc1NRHRDBGoGpZEXt_0WVZWEaTPDghvK-lfB2K6GYDN_zSs8pqeOzz9v29WJNDClFcGodh0nHK0WwupkatZmaIp9vOpr7Ceyd24xJAW8WkErIryDetfxnrWcL9TrPEW5r_Yr_ALsi0Tg</recordid><startdate>20050601</startdate><enddate>20050601</enddate><creator>Craig, Elizabeth A</creator><creator>Huang, Peggy</creator><creator>Gautschi, Matthias</creator><creator>Walter, William</creator><creator>Rospert, Sabine</creator><general>Nature Publishing Group US</general><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PADUT</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20050601</creationdate><title>The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1</title><author>Craig, Elizabeth A ; Huang, Peggy ; Gautschi, Matthias ; Walter, William ; Rospert, Sabine</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c520t-27afdd7bc816cfec85d787bc4fd0575cb236485b47e5136a6f8b2d8e906183dc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Adenosine Triphosphatases - 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Academic</collection><jtitle>Nature structural & molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Craig, Elizabeth A</au><au>Huang, Peggy</au><au>Gautschi, Matthias</au><au>Walter, William</au><au>Rospert, Sabine</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1</atitle><jtitle>Nature structural & molecular biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2005-06-01</date><risdate>2005</risdate><volume>12</volume><issue>6</issue><spage>497</spage><epage>504</epage><pages>497-504</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>J-proteins are obligate partners of Hsp70s, forming a ubiquitous class of molecular chaperone machinery. The ribosome-associated Hsp70 of yeast Ssb binds nascent polypeptides as they exit the ribosome. Here we report that the ribosome-associated J-protein Zuo1 is the partner of Ssb. However, Zuo1 efficiently stimulates the ATPase activity of Ssb only when in complex with another Hsp70, Ssz1. Ssz1 binds ATP, but none of the 11 different amino acid substitutions in the ATP-binding cleft affected Ssz1 function
in vivo
, suggesting that neither nucleotide binding nor hydrolysis is required. We propose that Ssz1's predominant function in the cell is to facilitate Zuo1's ability to function as a J-protein partner of Ssb on the ribosome, serving as an example of an Hsp70 family member that has evolved to carry out functions distinct from that of a chaperone.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>15908962</pmid><doi>10.1038/nsmb942</doi><tpages>8</tpages></addata></record> |
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| subjects | Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Amino acids ATP Biochemistry Biological Microscopy Biomedical and Life Sciences DNA binding proteins DNA-Binding Proteins - physiology HSP70 Heat-Shock Proteins - chemistry HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - metabolism HSP70 Heat-Shock Proteins - physiology Hydrolysis Kinetics Life Sciences Membrane Biology Models, Molecular Molecular Chaperones Phenotype Physiological aspects Polypeptides Protein Conformation Protein Structure Proteins Ribonucleic acid Ribosomes Ribosomes - metabolism RNA Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - physiology Structure Yeast Yeasts |
| title | The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1 |
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