Dynein from Dictyostelium: primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein
We report here the cloning and sequencing of a cytoplasmic dynein heavy chain gene from the cellular slime mold Dictyostelium discoideum. Using a combination of approaches, we have isolated 14,318 bp of DNA sequence which contains an open-reading frame of 4,725 amino acids. The deduced molecular wei...
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Veröffentlicht in: | The Journal of cell biology 1992-12, Vol.119 (6), p.1597-1604 |
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description | We report here the cloning and sequencing of a cytoplasmic dynein heavy chain gene from the cellular slime mold Dictyostelium discoideum. Using a combination of approaches, we have isolated 14,318 bp of DNA sequence which contains an open-reading frame of 4,725 amino acids. The deduced molecular weight of the polypeptide predicted by this reading frame is 538,482 D. Overall, the polypeptide sequence is 51% similar and 28% identical to the recently published sequences of the beta-dynein heavy chain from sea urchin flagella (Gibbons, I. R., B. H. Gibbons, G. Mocz, and D. J. Asai. 1991. Nature (Lond.). 352: 640-643; Ogawa, K. 1991. Nature (Lond.). 352:643-645). It contains four GXXXXGKT/S motifs that form part of a consensus sequence for ATP-binding domains; these motifs are clustered near the middle of the polypeptide. The distribution of the regions sharing sequence similarity between the Dictyostelium and sea urchin heavy chain polypeptides suggests that the amino termini of dyneins may contain domains that specify axonemal or cytoplasmic functions. |
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Richard</creator><creatorcontrib>Koonce, Michael P. ; Grissom, Paula M. ; McIntosh, J. Richard ; University of Colorado, Boulder, CO</creatorcontrib><description>We report here the cloning and sequencing of a cytoplasmic dynein heavy chain gene from the cellular slime mold Dictyostelium discoideum. Using a combination of approaches, we have isolated 14,318 bp of DNA sequence which contains an open-reading frame of 4,725 amino acids. The deduced molecular weight of the polypeptide predicted by this reading frame is 538,482 D. Overall, the polypeptide sequence is 51% similar and 28% identical to the recently published sequences of the beta-dynein heavy chain from sea urchin flagella (Gibbons, I. R., B. H. Gibbons, G. Mocz, and D. J. Asai. 1991. Nature (Lond.). 352: 640-643; Ogawa, K. 1991. Nature (Lond.). 352:643-645). It contains four GXXXXGKT/S motifs that form part of a consensus sequence for ATP-binding domains; these motifs are clustered near the middle of the polypeptide. The distribution of the regions sharing sequence similarity between the Dictyostelium and sea urchin heavy chain polypeptides suggests that the amino termini of dyneins may contain domains that specify axonemal or cytoplasmic functions.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.119.6.1597</identifier><identifier>PMID: 1469051</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>New York, NY: Rockefeller University Press</publisher><subject>Adenosine Triphosphate - metabolism ; adn ; Amino Acid Sequence ; Amino acids ; Animals ; Antiserum ; Base Sequence ; Biochemistry. Physiology. Immunology. Molecular biology ; Biological and medical sciences ; cell structure ; Cellular biology ; citoplasma ; Cloning, Molecular ; Consensus Sequence ; cytoplasm ; Cytoplasm - enzymology ; cytoplasme ; Deoxyribonucleic acid ; Dictyostelium - enzymology ; Dictyostelium - genetics ; DNA ; Dyneins - genetics ; Enzymes ; estructura celular ; Flagella - chemistry ; Fundamental and applied biological sciences. Psychology ; Gels ; gene ; Genes ; Genomics ; hidrolasas ; hydrolase ; hydrolases ; Invertebrates ; Microtubules ; mixomicetes ; Molecular Sequence Data ; Molecular Weight ; myxomycetes ; nucleotide ; nucleotides ; nucleotidos ; Open Reading Frames ; Polymerase chain reaction ; Protein Conformation ; Protein Structure, Secondary ; Protozoa ; Regional identity ; RNA ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; structure cellulaire</subject><ispartof>The Journal of cell biology, 1992-12, Vol.119 (6), p.1597-1604</ispartof><rights>Copyright 1992 The Rockefeller University Press</rights><rights>1993 INIST-CNRS</rights><rights>Copyright Rockefeller University Press Dec 1992</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c551t-5a4e4244817b5aafac0ee8d721cf297a5d6d41d38a12ff94eb6ee5e689dd4b393</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4576464$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1469051$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Koonce, Michael P.</creatorcontrib><creatorcontrib>Grissom, Paula M.</creatorcontrib><creatorcontrib>McIntosh, J. Richard</creatorcontrib><creatorcontrib>University of Colorado, Boulder, CO</creatorcontrib><title>Dynein from Dictyostelium: primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>We report here the cloning and sequencing of a cytoplasmic dynein heavy chain gene from the cellular slime mold Dictyostelium discoideum. Using a combination of approaches, we have isolated 14,318 bp of DNA sequence which contains an open-reading frame of 4,725 amino acids. The deduced molecular weight of the polypeptide predicted by this reading frame is 538,482 D. Overall, the polypeptide sequence is 51% similar and 28% identical to the recently published sequences of the beta-dynein heavy chain from sea urchin flagella (Gibbons, I. R., B. H. Gibbons, G. Mocz, and D. J. Asai. 1991. Nature (Lond.). 352: 640-643; Ogawa, K. 1991. Nature (Lond.). 352:643-645). It contains four GXXXXGKT/S motifs that form part of a consensus sequence for ATP-binding domains; these motifs are clustered near the middle of the polypeptide. The distribution of the regions sharing sequence similarity between the Dictyostelium and sea urchin heavy chain polypeptides suggests that the amino termini of dyneins may contain domains that specify axonemal or cytoplasmic functions.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>adn</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Antiserum</subject><subject>Base Sequence</subject><subject>Biochemistry. Physiology. Immunology. Molecular biology</subject><subject>Biological and medical sciences</subject><subject>cell structure</subject><subject>Cellular biology</subject><subject>citoplasma</subject><subject>Cloning, Molecular</subject><subject>Consensus Sequence</subject><subject>cytoplasm</subject><subject>Cytoplasm - enzymology</subject><subject>cytoplasme</subject><subject>Deoxyribonucleic acid</subject><subject>Dictyostelium - enzymology</subject><subject>Dictyostelium - genetics</subject><subject>DNA</subject><subject>Dyneins - genetics</subject><subject>Enzymes</subject><subject>estructura celular</subject><subject>Flagella - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>gene</subject><subject>Genes</subject><subject>Genomics</subject><subject>hidrolasas</subject><subject>hydrolase</subject><subject>hydrolases</subject><subject>Invertebrates</subject><subject>Microtubules</subject><subject>mixomicetes</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>myxomycetes</subject><subject>nucleotide</subject><subject>nucleotides</subject><subject>nucleotidos</subject><subject>Open Reading Frames</subject><subject>Polymerase chain reaction</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Protozoa</subject><subject>Regional identity</subject><subject>RNA</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>structure cellulaire</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkk1v1DAQhiMEKkvhygmQhRC3LJ7EdmIOSKjlS6rEAXq2Js5kySqxg52Awq_Hy65a4OTD-_j1jB5n2WPgW-B1-Wpvmy2A3qotSF3dyTYgBc9rEPxutuG8gFzLQt7PHsS455yLSpRn2RkIpbmETTZdro56x7rgR3bZ23n1caahX8bXbAr9iGFlcQ6LnZdAzPpxwtBH7yJraP5J5Bgyu85-GjCOvWWjn31g5H6tIzF0LesG3NEwYGDtn5ceZvc6HCI9Op3n2fX7d18vPuZXnz98unh7lVspYc4lChKFEDVUjUTs0HKiuq0KsF2hK5StagW0ZY1QdJ0W1CgiSarWbSuaUpfn2Ztj77Q0I7WW3BxwMKedjMfe_Ju4_pvZ-R-mKGpdKUgFL08FwX9fKM5m7KM9rOLIL9FUZVkLqMsEPv8P3PsluLScKaACfmAStD1CNvgYA3U3kwA3B5EmiTRJpFHmIDJdePr3_Lf40VzKX5xyjBaHLqCzfbzBhKyUUCJhT47YPiYxty0qfRPNU_zsGHfoDe6SWnP9BbQuOa8VV7r8DXNovHg</recordid><startdate>19921201</startdate><enddate>19921201</enddate><creator>Koonce, Michael P.</creator><creator>Grissom, Paula M.</creator><creator>McIntosh, J. Richard</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>FBQ</scope><scope>IQODW</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><scope>5PM</scope></search><sort><creationdate>19921201</creationdate><title>Dynein from Dictyostelium: primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein</title><author>Koonce, Michael P. ; Grissom, Paula M. ; McIntosh, J. Richard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c551t-5a4e4244817b5aafac0ee8d721cf297a5d6d41d38a12ff94eb6ee5e689dd4b393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>adn</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Antiserum</topic><topic>Base Sequence</topic><topic>Biochemistry. Physiology. Immunology. Molecular biology</topic><topic>Biological and medical sciences</topic><topic>cell structure</topic><topic>Cellular biology</topic><topic>citoplasma</topic><topic>Cloning, Molecular</topic><topic>Consensus Sequence</topic><topic>cytoplasm</topic><topic>Cytoplasm - enzymology</topic><topic>cytoplasme</topic><topic>Deoxyribonucleic acid</topic><topic>Dictyostelium - enzymology</topic><topic>Dictyostelium - genetics</topic><topic>DNA</topic><topic>Dyneins - genetics</topic><topic>Enzymes</topic><topic>estructura celular</topic><topic>Flagella - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>gene</topic><topic>Genes</topic><topic>Genomics</topic><topic>hidrolasas</topic><topic>hydrolase</topic><topic>hydrolases</topic><topic>Invertebrates</topic><topic>Microtubules</topic><topic>mixomicetes</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>myxomycetes</topic><topic>nucleotide</topic><topic>nucleotides</topic><topic>nucleotidos</topic><topic>Open Reading Frames</topic><topic>Polymerase chain reaction</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Protozoa</topic><topic>Regional identity</topic><topic>RNA</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>structure cellulaire</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Koonce, Michael P.</creatorcontrib><creatorcontrib>Grissom, Paula M.</creatorcontrib><creatorcontrib>McIntosh, J. Richard</creatorcontrib><creatorcontrib>University of Colorado, Boulder, CO</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Koonce, Michael P.</au><au>Grissom, Paula M.</au><au>McIntosh, J. Richard</au><aucorp>University of Colorado, Boulder, CO</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dynein from Dictyostelium: primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1992-12-01</date><risdate>1992</risdate><volume>119</volume><issue>6</issue><spage>1597</spage><epage>1604</epage><pages>1597-1604</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>We report here the cloning and sequencing of a cytoplasmic dynein heavy chain gene from the cellular slime mold Dictyostelium discoideum. Using a combination of approaches, we have isolated 14,318 bp of DNA sequence which contains an open-reading frame of 4,725 amino acids. The deduced molecular weight of the polypeptide predicted by this reading frame is 538,482 D. Overall, the polypeptide sequence is 51% similar and 28% identical to the recently published sequences of the beta-dynein heavy chain from sea urchin flagella (Gibbons, I. R., B. H. Gibbons, G. Mocz, and D. J. Asai. 1991. Nature (Lond.). 352: 640-643; Ogawa, K. 1991. Nature (Lond.). 352:643-645). It contains four GXXXXGKT/S motifs that form part of a consensus sequence for ATP-binding domains; these motifs are clustered near the middle of the polypeptide. The distribution of the regions sharing sequence similarity between the Dictyostelium and sea urchin heavy chain polypeptides suggests that the amino termini of dyneins may contain domains that specify axonemal or cytoplasmic functions.</abstract><cop>New York, NY</cop><pub>Rockefeller University Press</pub><pmid>1469051</pmid><doi>10.1083/jcb.119.6.1597</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adenosine Triphosphate - metabolism adn Amino Acid Sequence Amino acids Animals Antiserum Base Sequence Biochemistry. Physiology. Immunology. Molecular biology Biological and medical sciences cell structure Cellular biology citoplasma Cloning, Molecular Consensus Sequence cytoplasm Cytoplasm - enzymology cytoplasme Deoxyribonucleic acid Dictyostelium - enzymology Dictyostelium - genetics DNA Dyneins - genetics Enzymes estructura celular Flagella - chemistry Fundamental and applied biological sciences. Psychology Gels gene Genes Genomics hidrolasas hydrolase hydrolases Invertebrates Microtubules mixomicetes Molecular Sequence Data Molecular Weight myxomycetes nucleotide nucleotides nucleotidos Open Reading Frames Polymerase chain reaction Protein Conformation Protein Structure, Secondary Protozoa Regional identity RNA Sequence Analysis, DNA Sequence Homology, Amino Acid structure cellulaire |
title | Dynein from Dictyostelium: primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein |
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