Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity
As more data are generated from proteome and transcriptome analyses of snake venoms, we are gaining an appreciation of the complexity of the venoms and, to some degree, the various sources of such complexity. However, our knowledge is still far from complete. The translation of genetic information f...
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| Veröffentlicht in: | The FEBS journal 2008-06, Vol.275 (12), p.3016-3030 |
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| creator | Fox, Jay W Serrano, Solange M.T |
| description | As more data are generated from proteome and transcriptome analyses of snake venoms, we are gaining an appreciation of the complexity of the venoms and, to some degree, the various sources of such complexity. However, our knowledge is still far from complete. The translation of genetic information from the snake genome to the transcriptome and ultimately the proteome is only beginning to be appreciated, and will require significantly more investigation of the snake venom genomic structure prior to a complete understanding of the genesis of venom composition. Venom complexity, however, is derived not only from the venom genomic structure but also from transcriptome generation and translation and, perhaps most importantly, post-translation modification of the nascent venom proteome. In this review, we examine the snake venom metalloproteinases, some of the predominant components in viperid venoms, with regard to possible synthesis and post-translational mechanisms that contribute to venom complexity. The aim of this review is to highlight the state of our knowledge on snake venom metalloproteinase post-translational processing and to suggest testable hypotheses regarding the cellular mechanisms associated with snake venom metalloproteinase complexity in venoms. |
| doi_str_mv | 10.1111/j.1742-4658.2008.06466.x |
| format | Article |
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However, our knowledge is still far from complete. The translation of genetic information from the snake genome to the transcriptome and ultimately the proteome is only beginning to be appreciated, and will require significantly more investigation of the snake venom genomic structure prior to a complete understanding of the genesis of venom composition. Venom complexity, however, is derived not only from the venom genomic structure but also from transcriptome generation and translation and, perhaps most importantly, post-translation modification of the nascent venom proteome. In this review, we examine the snake venom metalloproteinases, some of the predominant components in viperid venoms, with regard to possible synthesis and post-translational mechanisms that contribute to venom complexity. The aim of this review is to highlight the state of our knowledge on snake venom metalloproteinase post-translational processing and to suggest testable hypotheses regarding the cellular mechanisms associated with snake venom metalloproteinase complexity in venoms.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>autolysis</subject><subject>Biochemistry</subject><subject>Chemical bonds</subject><subject>disintegrin</subject><subject>disulfide bond</subject><subject>Disulfides - chemistry</subject><subject>Genomics</subject><subject>Metalloproteases - chemistry</subject><subject>Metalloproteases - classification</subject><subject>Metalloproteases - metabolism</subject><subject>metalloproteinase</subject><subject>Molecular Sequence Data</subject><subject>post‐translational processing</subject><subject>Protein Folding</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Structure, Tertiary</subject><subject>proteome snake venom</subject><subject>Sequence Alignment</subject><subject>Snakes</subject><subject>structure</subject><subject>SVMP transcriptome</subject><subject>Toxicology</subject><subject>Viper Venoms - enzymology</subject><issn>1742-464X</issn><issn>1742-4658</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkV2P1CAUhhujcT_0LyjxwqyJM_JVCjeb6GZXN1mjybjGO0IpnWWkMBaqM__HHyptJ2vildxw4Lzn4XDeogAILlFebzZLVFG8oKzkSwwhX0JGGVvuHhTH94mH9zH9dlScxLiBkJRUiMfFEeK0EpTh4-L3tY92fZcisD4FoHwD4tbowalkg49A1WFIIHr13YCfxocOdCYp58K2D8lYr6IBZ6uvHz-_AnHv052JNr4GbXCN9esJ19g4uNY2BtQhH9vQdxN7SuYC2wMdfOptPUzXuYv5IR26rTM7m_ZPiketctE8Peynxe3V5ZeLD4ubT--vL97eLDRFgi2IEq2gnDBOWq41NsIYwThjpdCkLMs8KUbzSLASSIuaQ1WVHDGIat1ww1tyWrycuflzPwYTk-xs1MY55U0YoqxgxQXCJAtf_CPchKH3uTeJIUWYESyyiM8i3YcYe9PKbW871e8lgnK0UW7k6JAc3ZKjjXKyUe5y6bMDf6g70_wtPPiWBeez4Jd1Zv_fYHl1-W41hhnwfAa0Kki17m2UtysMEclqwSHF5A_qBrfK</recordid><startdate>200806</startdate><enddate>200806</enddate><creator>Fox, Jay W</creator><creator>Serrano, Solange M.T</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><scope>FBQ</scope><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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200806</creationdate><title>Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity</title><author>Fox, Jay W ; Serrano, Solange M.T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4196-3a9f9483683f8cc2e9ee9686659c3555200647422a91c9b80a7581601bcd8e8f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>autolysis</topic><topic>Biochemistry</topic><topic>Chemical bonds</topic><topic>disintegrin</topic><topic>disulfide bond</topic><topic>Disulfides - chemistry</topic><topic>Genomics</topic><topic>Metalloproteases - chemistry</topic><topic>Metalloproteases - classification</topic><topic>Metalloproteases - metabolism</topic><topic>metalloproteinase</topic><topic>Molecular Sequence Data</topic><topic>post‐translational processing</topic><topic>Protein Folding</topic><topic>Protein Processing, Post-Translational</topic><topic>Protein Structure, Tertiary</topic><topic>proteome snake venom</topic><topic>Sequence Alignment</topic><topic>Snakes</topic><topic>structure</topic><topic>SVMP transcriptome</topic><topic>Toxicology</topic><topic>Viper Venoms - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fox, Jay W</creatorcontrib><creatorcontrib>Serrano, Solange M.T</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The FEBS journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fox, Jay W</au><au>Serrano, Solange M.T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity</atitle><jtitle>The FEBS journal</jtitle><addtitle>FEBS J</addtitle><date>2008-06</date><risdate>2008</risdate><volume>275</volume><issue>12</issue><spage>3016</spage><epage>3030</epage><pages>3016-3030</pages><issn>1742-464X</issn><eissn>1742-4658</eissn><abstract>As more data are generated from proteome and transcriptome analyses of snake venoms, we are gaining an appreciation of the complexity of the venoms and, to some degree, the various sources of such complexity. However, our knowledge is still far from complete. The translation of genetic information from the snake genome to the transcriptome and ultimately the proteome is only beginning to be appreciated, and will require significantly more investigation of the snake venom genomic structure prior to a complete understanding of the genesis of venom composition. Venom complexity, however, is derived not only from the venom genomic structure but also from transcriptome generation and translation and, perhaps most importantly, post-translation modification of the nascent venom proteome. In this review, we examine the snake venom metalloproteinases, some of the predominant components in viperid venoms, with regard to possible synthesis and post-translational mechanisms that contribute to venom complexity. 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| subjects | Amino Acid Sequence Animals autolysis Biochemistry Chemical bonds disintegrin disulfide bond Disulfides - chemistry Genomics Metalloproteases - chemistry Metalloproteases - classification Metalloproteases - metabolism metalloproteinase Molecular Sequence Data post‐translational processing Protein Folding Protein Processing, Post-Translational Protein Structure, Tertiary proteome snake venom Sequence Alignment Snakes structure SVMP transcriptome Toxicology Viper Venoms - enzymology |
| title | Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity |
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