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
Hauptverfasser: Koonce, Michael P., Grissom, Paula M., McIntosh, J. Richard
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container_end_page 1604
container_issue 6
container_start_page 1597
container_title The Journal of cell biology
container_volume 119
creator Koonce, Michael P.
Grissom, Paula M.
McIntosh, J. Richard
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. 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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&amp;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. 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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. 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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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