Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1
Ribosomal protein S1 is an essential actor for protein synthesis in Escherichia coli . It is involved in mRNA recruitment by the 30S ribosomal subunit and recognition of the correct start codon during translation initiation. E. coli S1 is a modular protein that contains six repeats of an S1 motif, w...
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| Veröffentlicht in: | Biomolecular NMR assignments 2015-04, Vol.9 (1), p.107-111 |
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| creator | Giraud, Pierre Créchet, Jean-Bernard Uzan, Marc Bontems, François Sizun, Christina |
| description | Ribosomal protein S1 is an essential actor for protein synthesis in
Escherichia coli
. It is involved in mRNA recruitment by the 30S ribosomal subunit and recognition of the correct start codon during translation initiation.
E. coli
S1 is a modular protein that contains six repeats of an S1 motif, which have distinct functions despite structural homology. Whereas the three central repeats have been shown to be involved in mRNA recognition, the two first repeats that constitute the N-terminal domain of S1 are responsible for binding to the 30S subunit. Here we report the almost complete
1
H,
13
C and
15
N resonance assignment of two fragments of the 30S binding region of S1. The first fragment comprises only the first repeat. The second corresponds to the entire ribosome binding domain. Since S1 is absent from all high resolution X-ray structures of prokaryotic ribosomes, these data provide a first step towards atomic level structural characterization of this domain by NMR. Chemical shift analysis of the first repeat provides evidence for structural divergence from the canonical OB-fold of an S1 motif. In contrast the second domain displays the expected topology for an S1 motif, which rationalizes the functional specialization of the two subdomains. |
| doi_str_mv | 10.1007/s12104-014-9554-2 |
| format | Article |
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Escherichia coli
. It is involved in mRNA recruitment by the 30S ribosomal subunit and recognition of the correct start codon during translation initiation.
E. coli
S1 is a modular protein that contains six repeats of an S1 motif, which have distinct functions despite structural homology. Whereas the three central repeats have been shown to be involved in mRNA recognition, the two first repeats that constitute the N-terminal domain of S1 are responsible for binding to the 30S subunit. Here we report the almost complete
1
H,
13
C and
15
N resonance assignment of two fragments of the 30S binding region of S1. The first fragment comprises only the first repeat. The second corresponds to the entire ribosome binding domain. Since S1 is absent from all high resolution X-ray structures of prokaryotic ribosomes, these data provide a first step towards atomic level structural characterization of this domain by NMR. Chemical shift analysis of the first repeat provides evidence for structural divergence from the canonical OB-fold of an S1 motif. In contrast the second domain displays the expected topology for an S1 motif, which rationalizes the functional specialization of the two subdomains.</description><identifier>ISSN: 1874-2718</identifier><identifier>EISSN: 1874-270X</identifier><identifier>DOI: 10.1007/s12104-014-9554-2</identifier><identifier>PMID: 24682851</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Binding sites ; Biochemistry ; Biological and Medical Physics ; Biophysics ; Chemical Sciences ; E coli ; Escherichia coli ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - metabolism ; Molecular Sequence Data ; NMR ; Nuclear magnetic resonance ; Nuclear Magnetic Resonance, Biomolecular ; Physics ; Physics and Astronomy ; Polymer Sciences ; Protein Structure, Tertiary ; Proteins ; Ribosomal Proteins - chemistry ; Ribosomal Proteins - metabolism</subject><ispartof>Biomolecular NMR assignments, 2015-04, Vol.9 (1), p.107-111</ispartof><rights>Springer Science+Business Media Dordrecht 2014</rights><rights>Springer Science+Business Media Dordrecht 2015</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c476t-af7fbdb40b65d2ac3257d89bcd405c37701988f1da2ba32c284a477dc9ef0eec3</citedby><cites>FETCH-LOGICAL-c476t-af7fbdb40b65d2ac3257d89bcd405c37701988f1da2ba32c284a477dc9ef0eec3</cites><orcidid>0000-0002-4166-4845 ; 0000-0002-5760-2614</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12104-014-9554-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12104-014-9554-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24682851$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01138275$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Giraud, Pierre</creatorcontrib><creatorcontrib>Créchet, Jean-Bernard</creatorcontrib><creatorcontrib>Uzan, Marc</creatorcontrib><creatorcontrib>Bontems, François</creatorcontrib><creatorcontrib>Sizun, Christina</creatorcontrib><title>Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1</title><title>Biomolecular NMR assignments</title><addtitle>Biomol NMR Assign</addtitle><addtitle>Biomol NMR Assign</addtitle><description>Ribosomal protein S1 is an essential actor for protein synthesis in
Escherichia coli
. It is involved in mRNA recruitment by the 30S ribosomal subunit and recognition of the correct start codon during translation initiation.
E. coli
S1 is a modular protein that contains six repeats of an S1 motif, which have distinct functions despite structural homology. Whereas the three central repeats have been shown to be involved in mRNA recognition, the two first repeats that constitute the N-terminal domain of S1 are responsible for binding to the 30S subunit. Here we report the almost complete
1
H,
13
C and
15
N resonance assignment of two fragments of the 30S binding region of S1. The first fragment comprises only the first repeat. The second corresponds to the entire ribosome binding domain. Since S1 is absent from all high resolution X-ray structures of prokaryotic ribosomes, these data provide a first step towards atomic level structural characterization of this domain by NMR. Chemical shift analysis of the first repeat provides evidence for structural divergence from the canonical OB-fold of an S1 motif. In contrast the second domain displays the expected topology for an S1 motif, which rationalizes the functional specialization of the two subdomains.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Biological and Medical Physics</subject><subject>Biophysics</subject><subject>Chemical Sciences</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><subject>Polymer Sciences</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Ribosomal Proteins - chemistry</subject><subject>Ribosomal Proteins - metabolism</subject><issn>1874-2718</issn><issn>1874-270X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kUtLxDAUhYMovn-AGym40UX13jRtMksRXzAg-AB3IU3SMdIm2nQE_70p1UEEV7nkfPfkhEPIAcIpAvCziBSB5YAsn5Uly-ka2UbB08DheX01o9giOzG-AlQUKG6SLcoqQUWJ2-Th3sbgldc2UzG6he-sH7LQZMOLzXpXhxg6m9XOG-cXmQmdcn6UL08zHVr3g6g2e-vDYJP4gHtko1FttPvf5y55urp8vLjJ53fXtxfn81wzXg25anhTm5pBXZWGKl3Qkhsxq7VhUOqCc8CZEA0aRWtVUE0FU4xzo2e2AWt1sUtOJt8X1cq33nWq_5RBOXlzPpfjHSAWgvLyAxN7PLEp5vvSxkF2LmrbtsrbsIwSqwqLAgRWCT36g76GZe_TT0YKhOACeKJwonQfYuxts0qAIMd25NROCsHk2I6kaefw23lZd9asNn7qSACdgJgkv7D9r6f_df0CEaWYlg</recordid><startdate>20150401</startdate><enddate>20150401</enddate><creator>Giraud, Pierre</creator><creator>Créchet, Jean-Bernard</creator><creator>Uzan, Marc</creator><creator>Bontems, François</creator><creator>Sizun, Christina</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><general>Springer</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>K9.</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-4166-4845</orcidid><orcidid>https://orcid.org/0000-0002-5760-2614</orcidid></search><sort><creationdate>20150401</creationdate><title>Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1</title><author>Giraud, Pierre ; Créchet, Jean-Bernard ; Uzan, Marc ; Bontems, François ; Sizun, Christina</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c476t-af7fbdb40b65d2ac3257d89bcd405c37701988f1da2ba32c284a477dc9ef0eec3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Binding sites</topic><topic>Biochemistry</topic><topic>Biological and Medical Physics</topic><topic>Biophysics</topic><topic>Chemical Sciences</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>Physics</topic><topic>Physics and Astronomy</topic><topic>Polymer Sciences</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Ribosomal Proteins - chemistry</topic><topic>Ribosomal Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Giraud, Pierre</creatorcontrib><creatorcontrib>Créchet, Jean-Bernard</creatorcontrib><creatorcontrib>Uzan, Marc</creatorcontrib><creatorcontrib>Bontems, François</creatorcontrib><creatorcontrib>Sizun, Christina</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Biomolecular NMR assignments</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Giraud, Pierre</au><au>Créchet, Jean-Bernard</au><au>Uzan, Marc</au><au>Bontems, François</au><au>Sizun, Christina</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1</atitle><jtitle>Biomolecular NMR assignments</jtitle><stitle>Biomol NMR Assign</stitle><addtitle>Biomol NMR Assign</addtitle><date>2015-04-01</date><risdate>2015</risdate><volume>9</volume><issue>1</issue><spage>107</spage><epage>111</epage><pages>107-111</pages><issn>1874-2718</issn><eissn>1874-270X</eissn><abstract>Ribosomal protein S1 is an essential actor for protein synthesis in
Escherichia coli
. It is involved in mRNA recruitment by the 30S ribosomal subunit and recognition of the correct start codon during translation initiation.
E. coli
S1 is a modular protein that contains six repeats of an S1 motif, which have distinct functions despite structural homology. Whereas the three central repeats have been shown to be involved in mRNA recognition, the two first repeats that constitute the N-terminal domain of S1 are responsible for binding to the 30S subunit. Here we report the almost complete
1
H,
13
C and
15
N resonance assignment of two fragments of the 30S binding region of S1. The first fragment comprises only the first repeat. The second corresponds to the entire ribosome binding domain. Since S1 is absent from all high resolution X-ray structures of prokaryotic ribosomes, these data provide a first step towards atomic level structural characterization of this domain by NMR. Chemical shift analysis of the first repeat provides evidence for structural divergence from the canonical OB-fold of an S1 motif. In contrast the second domain displays the expected topology for an S1 motif, which rationalizes the functional specialization of the two subdomains.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>24682851</pmid><doi>10.1007/s12104-014-9554-2</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0002-4166-4845</orcidid><orcidid>https://orcid.org/0000-0002-5760-2614</orcidid></addata></record> |
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| subjects | Amino Acid Motifs Amino Acid Sequence Binding sites Biochemistry Biological and Medical Physics Biophysics Chemical Sciences E coli Escherichia coli Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Molecular Sequence Data NMR Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Physics Physics and Astronomy Polymer Sciences Protein Structure, Tertiary Proteins Ribosomal Proteins - chemistry Ribosomal Proteins - metabolism |
| title | Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1 |
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