Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein.
Identifieur interne : 001845 ( PubMed/Corpus ); précédent : 001844; suivant : 001846Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein.
Auteurs : Chun-Yu Huang ; Yen-Lan Hsu ; Wan-Ling Chiang ; Ming-Hon HouSource :
- Protein science : a publication of the Protein Society [ 1469-896X ] ; 2009.
English descriptors
- KwdEn :
- Binding Sites, Circular Dichroism, Coronavirus OC43, Human (chemistry), Glutaral (chemistry), Humans, Nucleic Acids (metabolism), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Protein Multimerization, Protein Stability, RNA-Binding Proteins (chemistry), RNA-Binding Proteins (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Spectrometry, Fluorescence, Urea (chemistry).
- MESH :
- chemical , chemistry : Glutaral, Nucleocapsid Proteins, RNA-Binding Proteins, Recombinant Proteins, Urea.
- chemistry : Coronavirus OC43, Human.
- chemical , metabolism : Nucleic Acids, Nucleocapsid Proteins, RNA-Binding Proteins, Recombinant Proteins.
- Binding Sites, Circular Dichroism, Humans, Protein Multimerization, Protein Stability, Spectrometry, Fluorescence.
Abstract
Human coronavirus OC43 (HCoV-OC43) is one of the causes of the "common cold" in human during seasons of cold weather. The primary function of the HCoV-OC43 nucleocapsid protein (N protein) is to recognize viral genomic RNA, which leads to ribonucleocapsid formation. Here, we characterized the stability and identified the functional regions of the recombinant HCoV-OC43 N protein. Circular dichroism and fluorescence measurements revealed that the HCoV-OC43 N protein is more highly ordered and stabler than the SARS-CoV N protein previously studied. Surface plasmon resonance (SPR) experiments showed that the affinity of HCoV-OC43 N protein for RNA was approximately fivefold higher than that of N protein for DNA. Moreover, we found that the HCoV-OC43 N protein contains three RNA-binding regions in its N-terminal region (residues 1-173) and central-linker region (residues 174-232 and 233-300). The binding affinities of the truncated N proteins and RNA follow the order: residues 1-173-residues 233-300 > residues 174-232. SPR experiments demonstrated that the C-terminal region (residues 301-448) of HCoV-OC43 N protein lacks RNA-binding activity, while crosslinking and gel filtration analyses revealed that the C-terminal region is mainly involved in the oligomerization of the HCoV-OC43 N protein. This study may benefit the understanding of the mechanism of HCoV-OC43 nucleocapsid formation.
DOI: 10.1002/pro.225
PubMed: 19691129
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The primary function of the HCoV-OC43 nucleocapsid protein (N protein) is to recognize viral genomic RNA, which leads to ribonucleocapsid formation. Here, we characterized the stability and identified the functional regions of the recombinant HCoV-OC43 N protein. Circular dichroism and fluorescence measurements revealed that the HCoV-OC43 N protein is more highly ordered and stabler than the SARS-CoV N protein previously studied. Surface plasmon resonance (SPR) experiments showed that the affinity of HCoV-OC43 N protein for RNA was approximately fivefold higher than that of N protein for DNA. Moreover, we found that the HCoV-OC43 N protein contains three RNA-binding regions in its N-terminal region (residues 1-173) and central-linker region (residues 174-232 and 233-300). The binding affinities of the truncated N proteins and RNA follow the order: residues 1-173-residues 233-300 > residues 174-232. SPR experiments demonstrated that the C-terminal region (residues 301-448) of HCoV-OC43 N protein lacks RNA-binding activity, while crosslinking and gel filtration analyses revealed that the C-terminal region is mainly involved in the oligomerization of the HCoV-OC43 N protein. This study may benefit the understanding of the mechanism of HCoV-OC43 nucleocapsid formation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19691129</PMID><DateCompleted><Year>2010</Year><Month>02</Month><Day>12</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1469-896X</ISSN><JournalIssue CitedMedium="Internet"><Volume>18</Volume><Issue>11</Issue><PubDate><Year>2009</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Protein science : a publication of the Protein Society</Title><ISOAbbreviation>Protein Sci.</ISOAbbreviation></Journal><ArticleTitle>Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein.</ArticleTitle><Pagination><MedlinePgn>2209-18</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/pro.225</ELocationID><Abstract><AbstractText>Human coronavirus OC43 (HCoV-OC43) is one of the causes of the "common cold" in human during seasons of cold weather. The primary function of the HCoV-OC43 nucleocapsid protein (N protein) is to recognize viral genomic RNA, which leads to ribonucleocapsid formation. Here, we characterized the stability and identified the functional regions of the recombinant HCoV-OC43 N protein. Circular dichroism and fluorescence measurements revealed that the HCoV-OC43 N protein is more highly ordered and stabler than the SARS-CoV N protein previously studied. Surface plasmon resonance (SPR) experiments showed that the affinity of HCoV-OC43 N protein for RNA was approximately fivefold higher than that of N protein for DNA. Moreover, we found that the HCoV-OC43 N protein contains three RNA-binding regions in its N-terminal region (residues 1-173) and central-linker region (residues 174-232 and 233-300). The binding affinities of the truncated N proteins and RNA follow the order: residues 1-173-residues 233-300 > residues 174-232. SPR experiments demonstrated that the C-terminal region (residues 301-448) of HCoV-OC43 N protein lacks RNA-binding activity, while crosslinking and gel filtration analyses revealed that the C-terminal region is mainly involved in the oligomerization of the HCoV-OC43 N protein. This study may benefit the understanding of the mechanism of HCoV-OC43 nucleocapsid formation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Huang</LastName><ForeName>Chun-Yu</ForeName><Initials>CY</Initials><AffiliationInfo><Affiliation>Biotechnology Center, National Chung Hsing University, Taichung 402, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hsu</LastName><ForeName>Yen-Lan</ForeName><Initials>YL</Initials></Author><Author ValidYN="Y"><LastName>Chiang</LastName><ForeName>Wan-Ling</ForeName><Initials>WL</Initials></Author><Author ValidYN="Y"><LastName>Hou</LastName><ForeName>Ming-Hon</ForeName><Initials>MH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United 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14;349(7):709</Citation><ArticleIdList><ArticleId IdType="pubmed">12917313</ArticleId></ArticleIdList></Reference><Reference><Citation>Clin Infect Dis. 2003 Apr 15;36(8):985-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12684910</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2004 Aug;78(16):8824-34</Citation><ArticleIdList><ArticleId IdType="pubmed">15280490</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2004 Aug 31;43(34):11103-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15323569</ArticleId></ArticleIdList></Reference><Reference><Citation>Am Rev Respir Dis. 1974 Jun;109(6):621-4</Citation><ArticleIdList><ArticleId IdType="pubmed">4365165</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 1983 Oct 30;130(2):527-32</Citation><ArticleIdList><ArticleId IdType="pubmed">6196910</ArticleId></ArticleIdList></Reference><Reference><Citation>Virus Res. 1986 Aug;5(2-3):131-44</Citation><ArticleIdList><ArticleId IdType="pubmed">3765820</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 1988 Nov;62(11):4280-7</Citation><ArticleIdList><ArticleId IdType="pubmed">2845140</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1988 Oct 18;27(21):8069-74</Citation><ArticleIdList><ArticleId IdType="pubmed">3233196</ArticleId></ArticleIdList></Reference><Reference><Citation>Virus Res. 1989 Jan;12(1):1-9</Citation><ArticleIdList><ArticleId IdType="pubmed">2541577</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 1991 May 6;282(2):419-24</Citation><ArticleIdList><ArticleId IdType="pubmed">1674698</ArticleId></ArticleIdList></Reference><Reference><Citation>Adv Exp Med Biol. 1990;276:235-8</Citation><ArticleIdList><ArticleId IdType="pubmed">1715663</ArticleId></ArticleIdList></Reference><Reference><Citation>Adv Exp Med Biol. 1990;276:239-46</Citation><ArticleIdList><ArticleId IdType="pubmed">1966408</ArticleId></ArticleIdList></Reference><Reference><Citation>Adv Exp Med Biol. 1990;276:247-54</Citation><ArticleIdList><ArticleId IdType="pubmed">1966409</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Virol. 1992;125(1-4):141-60</Citation><ArticleIdList><ArticleId IdType="pubmed">1322650</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1993 Feb 15;209(1):32-44</Citation><ArticleIdList><ArticleId IdType="pubmed">8465960</ArticleId></ArticleIdList></Reference><Reference><Citation>J Gen Virol. 1993 Sep;74 ( Pt 9):1975-9</Citation><ArticleIdList><ArticleId IdType="pubmed">8397288</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 1995 Sep;69(9):5475-84</Citation><ArticleIdList><ArticleId IdType="pubmed">7636993</ArticleId></ArticleIdList></Reference><Reference><Citation>Adv Virus Res. 1997;48:1-100</Citation><ArticleIdList><ArticleId IdType="pubmed">9233431</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2005 Jan;79(2):1164-79</Citation><ArticleIdList><ArticleId IdType="pubmed">15613344</ArticleId></ArticleIdList></Reference><Reference><Citation>Proteomics. 2005 Mar;5(4):925-37</Citation><ArticleIdList><ArticleId IdType="pubmed">15759315</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2005 Jun 17;280(24):23280-6</Citation><ArticleIdList><ArticleId IdType="pubmed">15849181</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 2005 Oct 24;579(25):5663-8</Citation><ArticleIdList><ArticleId IdType="pubmed">16214138</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2005 Nov;79(22):13848-55</Citation><ArticleIdList><ArticleId IdType="pubmed">16254320</ArticleId></ArticleIdList></Reference><Reference><Citation>Clin Diagn Lab Immunol. 2005 Nov;12(11):1317-21</Citation><ArticleIdList><ArticleId IdType="pubmed">16275947</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2005 Nov 22;44(46):15351-8</Citation><ArticleIdList><ArticleId IdType="pubmed">16285739</ArticleId></ArticleIdList></Reference><Reference><Citation>Virol J. 2004;1:7</Citation><ArticleIdList><ArticleId IdType="pubmed">15548333</ArticleId></ArticleIdList></Reference><Reference><Citation>Structure. 2005 Dec;13(12):1859-68</Citation><ArticleIdList><ArticleId IdType="pubmed">16338414</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biomed Sci. 2006 Jan;13(1):59-72</Citation><ArticleIdList><ArticleId IdType="pubmed">16228284</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Apr 21;281(16):10669-81</Citation><ArticleIdList><ArticleId IdType="pubmed">16431923</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2006 Jul;80(13):6612-20</Citation><ArticleIdList><ArticleId IdType="pubmed">16775348</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Jun 23;281(25):17134-9</Citation><ArticleIdList><ArticleId IdType="pubmed">16627473</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2006 Oct 3;45(39):11827-35</Citation><ArticleIdList><ArticleId IdType="pubmed">17002283</ArticleId></ArticleIdList></Reference><Reference><Citation>Adv Exp Med Biol. 2006;581:313-8</Citation><ArticleIdList><ArticleId IdType="pubmed">17037551</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 2006 Oct 30;580(25):5993-8</Citation><ArticleIdList><ArticleId IdType="pubmed">17052713</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2007 Jan 20;357(2):215-27</Citation><ArticleIdList><ArticleId IdType="pubmed">16979208</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2007 Jan;81(1):20-9</Citation><ArticleIdList><ArticleId IdType="pubmed">16928755</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2007 Jan;81(2):548-57</Citation><ArticleIdList><ArticleId IdType="pubmed">17108024</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol Methods. 2007 Feb;139(2):175-80</Citation><ArticleIdList><ArticleId IdType="pubmed">17079026</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Rev Microbiol. 2007 Feb;5(2):119-27</Citation><ArticleIdList><ArticleId IdType="pubmed">17224921</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2007 Apr;81(8):3913-21</Citation><ArticleIdList><ArticleId IdType="pubmed">17229691</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2007 May 11;368(4):1075-86</Citation><ArticleIdList><ArticleId IdType="pubmed">17379242</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2008 Jan 20;370(2):373-81</Citation><ArticleIdList><ArticleId IdType="pubmed">17931676</ArticleId></ArticleIdList></Reference><Reference><Citation>Vaccine. 2008 Mar 20;26(13):1644-51</Citation><ArticleIdList><ArticleId IdType="pubmed">18289745</ArticleId></ArticleIdList></Reference><Reference><Citation>Adv Exp Med Biol. 2007;623:107-22</Citation><ArticleIdList><ArticleId IdType="pubmed">18380343</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 2008 Jul 18;380(4):608-22</Citation><ArticleIdList><ArticleId IdType="pubmed">18561946</ArticleId></ArticleIdList></Reference><Reference><Citation>J Gen Virol. 2000 Jan;81(Pt 1):181-8</Citation><ArticleIdList><ArticleId IdType="pubmed">10640556</ArticleId></ArticleIdList></Reference><Reference><Citation>Clin Infect Dis. 2000 Jul;31(1):96-100</Citation><ArticleIdList><ArticleId IdType="pubmed">10913403</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2000 Oct;74(19):8913-21</Citation><ArticleIdList><ArticleId IdType="pubmed">10982334</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2000 Nov;74(22):10571-80</Citation><ArticleIdList><ArticleId IdType="pubmed">11044101</ArticleId></ArticleIdList></Reference><Reference><Citation>J Hosp Infect. 2002 May;51(1):59-64</Citation><ArticleIdList><ArticleId IdType="pubmed">12009822</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2004 May 25;43(20):6059-63</Citation><ArticleIdList><ArticleId IdType="pubmed">15147189</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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