Conserved Structural and Sequence Elements Implicated in the Processing of Gene-encoded Circular Proteins
The cyclotides are the largest family of naturally occurring circular proteins. The mechanism by which the termini of these gene-encoded proteins are linked seamlessly with a peptide bond to form a circular backbone is unknown. Here we report cyclotide-encoding cDNA sequences from the plant Viola od...
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| Veröffentlicht in: | The Journal of biological chemistry 2004-11, Vol.279 (45), p.46858-46867 |
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| container_end_page | 46867 |
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| container_issue | 45 |
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| container_title | The Journal of biological chemistry |
| container_volume | 279 |
| creator | Dutton, Julie L Renda, Rosemary F Waine, Clement Clark, Richard J Daly, Norelle L Jennings, Cameron V Anderson, Marilyn A Craik, David J |
| description | The cyclotides are the largest family of naturally occurring circular proteins. The mechanism by which the termini of these
gene-encoded proteins are linked seamlessly with a peptide bond to form a circular backbone is unknown. Here we report cyclotide-encoding
cDNA sequences from the plant Viola odorata and compare them with those from an evolutionarily distinct species, Oldenlandia affinis . Individual members of this multigene family encode one to three mature cyclotide domains. These domains are preceded by
N-terminal repeat regions (NTRs) that are conserved within a plant species but not between species. We have structurally characterized
peptides corresponding to these NTRs and show that, despite them having no sequence homology, they form a structurally conserved
α-helical motif. This structural conservation suggests a vital role for the NTR in the in vivo folding, processing, or detoxification of cyclotide domains from the precursor protein. |
| doi_str_mv | 10.1074/jbc.M407421200 |
| format | Article |
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gene-encoded proteins are linked seamlessly with a peptide bond to form a circular backbone is unknown. Here we report cyclotide-encoding
cDNA sequences from the plant Viola odorata and compare them with those from an evolutionarily distinct species, Oldenlandia affinis . Individual members of this multigene family encode one to three mature cyclotide domains. These domains are preceded by
N-terminal repeat regions (NTRs) that are conserved within a plant species but not between species. We have structurally characterized
peptides corresponding to these NTRs and show that, despite them having no sequence homology, they form a structurally conserved
α-helical motif. This structural conservation suggests a vital role for the NTR in the in vivo folding, processing, or detoxification of cyclotide domains from the precursor protein.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M407421200</identifier><identifier>PMID: 15328347</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Animals ; Asteraceae ; Conserved Sequence ; Crystallography, X-Ray ; Cyclotides - chemistry ; DNA, Complementary - chemistry ; DNA, Complementary - metabolism ; Evolution, Molecular ; Genes, Plant ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Multigene Family ; Oldenlandia ; Peptides - chemistry ; Protein Conformation ; Protein Folding ; Protein Structure, Tertiary ; Protons ; RNA - chemistry ; Sequence Homology, Amino Acid ; Viola ; Viola odorata</subject><ispartof>The Journal of biological chemistry, 2004-11, Vol.279 (45), p.46858-46867</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c323t-6f8bc3299f090fda905fb444e642633993f9a27a1db4ab8e773bb9d02c0f80063</citedby><cites>FETCH-LOGICAL-c323t-6f8bc3299f090fda905fb444e642633993f9a27a1db4ab8e773bb9d02c0f80063</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15328347$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dutton, Julie L</creatorcontrib><creatorcontrib>Renda, Rosemary F</creatorcontrib><creatorcontrib>Waine, Clement</creatorcontrib><creatorcontrib>Clark, Richard J</creatorcontrib><creatorcontrib>Daly, Norelle L</creatorcontrib><creatorcontrib>Jennings, Cameron V</creatorcontrib><creatorcontrib>Anderson, Marilyn A</creatorcontrib><creatorcontrib>Craik, David J</creatorcontrib><title>Conserved Structural and Sequence Elements Implicated in the Processing of Gene-encoded Circular Proteins</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The cyclotides are the largest family of naturally occurring circular proteins. The mechanism by which the termini of these
gene-encoded proteins are linked seamlessly with a peptide bond to form a circular backbone is unknown. Here we report cyclotide-encoding
cDNA sequences from the plant Viola odorata and compare them with those from an evolutionarily distinct species, Oldenlandia affinis . Individual members of this multigene family encode one to three mature cyclotide domains. These domains are preceded by
N-terminal repeat regions (NTRs) that are conserved within a plant species but not between species. We have structurally characterized
peptides corresponding to these NTRs and show that, despite them having no sequence homology, they form a structurally conserved
α-helical motif. This structural conservation suggests a vital role for the NTR in the in vivo folding, processing, or detoxification of cyclotide domains from the precursor protein.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Asteraceae</subject><subject>Conserved Sequence</subject><subject>Crystallography, X-Ray</subject><subject>Cyclotides - chemistry</subject><subject>DNA, Complementary - chemistry</subject><subject>DNA, Complementary - metabolism</subject><subject>Evolution, Molecular</subject><subject>Genes, Plant</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Multigene Family</subject><subject>Oldenlandia</subject><subject>Peptides - chemistry</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein Structure, Tertiary</subject><subject>Protons</subject><subject>RNA - chemistry</subject><subject>Sequence Homology, Amino Acid</subject><subject>Viola</subject><subject>Viola odorata</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c9rFDEUB_Agil2rV48yB_E268uPmSRHWWotVCy0greQZF66KTOZNZlR-t-bsgs9mkte4PMevHwJeU9hS0GKzw_Ob7-LWjHKAF6QDQXFW97RXy_JBoDRVrNOnZE3pTxAPULT1-SMdpwpLuSGxN2cCuY_ODS3S179smY7NjbVJ_5eMXlsLkacMC2luZoOY_R2qTamZtljc5Nnj6XEdN_MobnEhG1tmYcqdjH7dbT5ySwYU3lLXgU7Fnx3us_Jz68Xd7tv7fWPy6vdl-vWc8aXtg_K1UrrABrCYDV0wQkhsBes51xrHrRl0tLBCesUSsmd0wMwD0EB9PycfDrOPeS5blAWM8XicRxtwnktppfAeCfgv5BKyZToWYXbI_R5LiVjMIccJ5sfDQXzlIKpKZjnFGrDh9Pk1U04PPPTt1fw8Qj28X7_N2Y0Ls5-j5NhUhvRGdGrTvF_K3ePPg</recordid><startdate>20041105</startdate><enddate>20041105</enddate><creator>Dutton, Julie L</creator><creator>Renda, Rosemary F</creator><creator>Waine, Clement</creator><creator>Clark, Richard J</creator><creator>Daly, Norelle L</creator><creator>Jennings, Cameron V</creator><creator>Anderson, Marilyn A</creator><creator>Craik, David J</creator><general>American Society for Biochemistry and Molecular Biology</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>20041105</creationdate><title>Conserved Structural and Sequence Elements Implicated in the Processing of Gene-encoded Circular Proteins</title><author>Dutton, Julie L ; Renda, Rosemary F ; Waine, Clement ; Clark, Richard J ; Daly, Norelle L ; Jennings, Cameron V ; Anderson, Marilyn A ; Craik, David J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c323t-6f8bc3299f090fda905fb444e642633993f9a27a1db4ab8e773bb9d02c0f80063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Asteraceae</topic><topic>Conserved Sequence</topic><topic>Crystallography, X-Ray</topic><topic>Cyclotides - chemistry</topic><topic>DNA, Complementary - chemistry</topic><topic>DNA, Complementary - metabolism</topic><topic>Evolution, Molecular</topic><topic>Genes, Plant</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Multigene Family</topic><topic>Oldenlandia</topic><topic>Peptides - chemistry</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Protein Structure, Tertiary</topic><topic>Protons</topic><topic>RNA - chemistry</topic><topic>Sequence Homology, Amino Acid</topic><topic>Viola</topic><topic>Viola odorata</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dutton, Julie L</creatorcontrib><creatorcontrib>Renda, Rosemary F</creatorcontrib><creatorcontrib>Waine, Clement</creatorcontrib><creatorcontrib>Clark, Richard J</creatorcontrib><creatorcontrib>Daly, Norelle L</creatorcontrib><creatorcontrib>Jennings, Cameron V</creatorcontrib><creatorcontrib>Anderson, Marilyn A</creatorcontrib><creatorcontrib>Craik, David J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dutton, Julie L</au><au>Renda, Rosemary F</au><au>Waine, Clement</au><au>Clark, Richard J</au><au>Daly, Norelle L</au><au>Jennings, Cameron V</au><au>Anderson, Marilyn A</au><au>Craik, David J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conserved Structural and Sequence Elements Implicated in the Processing of Gene-encoded Circular Proteins</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-11-05</date><risdate>2004</risdate><volume>279</volume><issue>45</issue><spage>46858</spage><epage>46867</epage><pages>46858-46867</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The cyclotides are the largest family of naturally occurring circular proteins. The mechanism by which the termini of these
gene-encoded proteins are linked seamlessly with a peptide bond to form a circular backbone is unknown. Here we report cyclotide-encoding
cDNA sequences from the plant Viola odorata and compare them with those from an evolutionarily distinct species, Oldenlandia affinis . Individual members of this multigene family encode one to three mature cyclotide domains. These domains are preceded by
N-terminal repeat regions (NTRs) that are conserved within a plant species but not between species. We have structurally characterized
peptides corresponding to these NTRs and show that, despite them having no sequence homology, they form a structurally conserved
α-helical motif. This structural conservation suggests a vital role for the NTR in the in vivo folding, processing, or detoxification of cyclotide domains from the precursor protein.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>15328347</pmid><doi>10.1074/jbc.M407421200</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Asteraceae Conserved Sequence Crystallography, X-Ray Cyclotides - chemistry DNA, Complementary - chemistry DNA, Complementary - metabolism Evolution, Molecular Genes, Plant Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Multigene Family Oldenlandia Peptides - chemistry Protein Conformation Protein Folding Protein Structure, Tertiary Protons RNA - chemistry Sequence Homology, Amino Acid Viola Viola odorata |
| title | Conserved Structural and Sequence Elements Implicated in the Processing of Gene-encoded Circular Proteins |
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