Nucleotide exchange, structure, and mechanical properties of filaments assembled from ATP-actin and ADP-actin
Actin monomers with bound ATP, ADP, or fluorescent analogues of these nucleotides exchange the nucleotide on a second time scale, whereas filaments assembled from each of these species exchange their nucleotide with the solution at least 1,000 times slower than monomers. Filaments assembled from eit...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-10, Vol.267 (28), p.20339-20345 |
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| container_title | The Journal of biological chemistry |
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| creator | POLLARD, TD GOLDBERG SCHWARZ, WH |
| description | Actin monomers with bound ATP, ADP, or fluorescent analogues of these nucleotides exchange the nucleotide on a second time
scale, whereas filaments assembled from each of these species exchange their nucleotide with the solution at least 1,000 times
slower than monomers. Filaments assembled from either ATP-actin or ADP-actin are indistinguishable by electron microscopy
after negative staining. The dynamic elasticity and viscosity of filaments assembled from ATP-actin or ADP-actin or mixtures
of these two species are the same over a wide range of frequencies. These observations do not support a recent suggestion
(Janmey, P. A., Hvidt, S., Oster, G. F., Lamb, J., Stossel, T. P., and Hartwig, J. H. (1990) Nature 347, 95-99) that ATP hydrolysis
within actin filaments stiffens the polymer and alters both their structure and affinity for nucleotides. The difference in
observations between these two studies may be related to time-dependent changes in ADP-actin prepared in slightly different
ways. |
| doi_str_mv | 10.1016/s0021-9258(19)88707-0 |
| format | Article |
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scale, whereas filaments assembled from each of these species exchange their nucleotide with the solution at least 1,000 times
slower than monomers. Filaments assembled from either ATP-actin or ADP-actin are indistinguishable by electron microscopy
after negative staining. The dynamic elasticity and viscosity of filaments assembled from ATP-actin or ADP-actin or mixtures
of these two species are the same over a wide range of frequencies. These observations do not support a recent suggestion
(Janmey, P. A., Hvidt, S., Oster, G. F., Lamb, J., Stossel, T. P., and Hartwig, J. H. (1990) Nature 347, 95-99) that ATP hydrolysis
within actin filaments stiffens the polymer and alters both their structure and affinity for nucleotides. The difference in
observations between these two studies may be related to time-dependent changes in ADP-actin prepared in slightly different
ways.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(19)88707-0</identifier><identifier>PMID: 1400353</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>BETHESDA: American Society for Biochemistry and Molecular Biology</publisher><subject>actin ; Actin Cytoskeleton - chemistry ; Actin Cytoskeleton - ultrastructure ; Actins - chemistry ; Adenosine Diphosphate - analogs & derivatives ; Adenosine Diphosphate - chemistry ; Adenosine Triphosphate - analogs & derivatives ; Adenosine Triphosphate - chemistry ; ADP ; Analytical, structural and metabolic biochemistry ; Animals ; ATP ; binding ; Biochemistry & Molecular Biology ; Biological and medical sciences ; Biomechanical Phenomena ; Biopolymers ; Contractile proteins ; Fundamental and applied biological sciences. Psychology ; Holoproteins ; Kinetics ; Life Sciences & Biomedicine ; Microscopy, Electron ; Muscles - chemistry ; Nucleotides - chemistry ; Proteins ; Rabbits ; Science & Technology ; skeletal muscle</subject><ispartof>The Journal of biological chemistry, 1992-10, Vol.267 (28), p.20339-20345</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>86</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wosA1992JR85800093</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c506t-201592c6a7dd656a0945d1ac53280de373a0075c19c43ceab4f9a78ac68fcf233</citedby><cites>FETCH-LOGICAL-c506t-201592c6a7dd656a0945d1ac53280de373a0075c19c43ceab4f9a78ac68fcf233</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,27201,27933,27934</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4401988$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1400353$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>POLLARD, TD</creatorcontrib><creatorcontrib>GOLDBERG</creatorcontrib><creatorcontrib>SCHWARZ, WH</creatorcontrib><title>Nucleotide exchange, structure, and mechanical properties of filaments assembled from ATP-actin and ADP-actin</title><title>The Journal of biological chemistry</title><addtitle>J BIOL CHEM</addtitle><addtitle>J Biol Chem</addtitle><description>Actin monomers with bound ATP, ADP, or fluorescent analogues of these nucleotides exchange the nucleotide on a second time
scale, whereas filaments assembled from each of these species exchange their nucleotide with the solution at least 1,000 times
slower than monomers. Filaments assembled from either ATP-actin or ADP-actin are indistinguishable by electron microscopy
after negative staining. The dynamic elasticity and viscosity of filaments assembled from ATP-actin or ADP-actin or mixtures
of these two species are the same over a wide range of frequencies. These observations do not support a recent suggestion
(Janmey, P. A., Hvidt, S., Oster, G. F., Lamb, J., Stossel, T. P., and Hartwig, J. H. (1990) Nature 347, 95-99) that ATP hydrolysis
within actin filaments stiffens the polymer and alters both their structure and affinity for nucleotides. The difference in
observations between these two studies may be related to time-dependent changes in ADP-actin prepared in slightly different
ways.</description><subject>actin</subject><subject>Actin Cytoskeleton - chemistry</subject><subject>Actin Cytoskeleton - ultrastructure</subject><subject>Actins - chemistry</subject><subject>Adenosine Diphosphate - analogs & derivatives</subject><subject>Adenosine Diphosphate - chemistry</subject><subject>Adenosine Triphosphate - analogs & derivatives</subject><subject>Adenosine Triphosphate - chemistry</subject><subject>ADP</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>ATP</subject><subject>binding</subject><subject>Biochemistry & Molecular Biology</subject><subject>Biological and medical sciences</subject><subject>Biomechanical Phenomena</subject><subject>Biopolymers</subject><subject>Contractile proteins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Holoproteins</subject><subject>Kinetics</subject><subject>Life Sciences & Biomedicine</subject><subject>Microscopy, Electron</subject><subject>Muscles - chemistry</subject><subject>Nucleotides - chemistry</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Science & Technology</subject><subject>skeletal muscle</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EZCTM</sourceid><sourceid>EIF</sourceid><recordid>eNqNkV9vFCEUxYnR1G31IzSZB2M0OnqBYQYeN2v9l0aN1sQ3wjKXLmZmWIFJ9dvLdjfbR-UFyPkduDmHkHMKryjQ9nUCYLRWTMhnVD2XsoOuhntkQUHymgv64z5ZHJGH5DSln1BWo-gJOaENABd8QcZPsx0wZN9jhb_txkzX-LJKOc42z7EczdRXI-4Eb81QbWPYYsweUxVc5fxgRpxyqkxKOK4H7CsXw1gtr77UxmY_3fqXbw63R-SBM0PCx4f9jHx_e3G1el9ffn73YbW8rK2ANtcMqFDMtqbr-1a0BlQjemqs4ExCj7zjBqATlirbcItm3ThlOmlsK511jPMz8nT_bhn314wp69Eni8NgJgxz0h1nDQhQ_wRp2yipaFtAsQdtDClFdHob_WjiH01B7_rQ33Zh613Ymip924eG4js_fDCvR-zvXPsCiv7koJtU8nXRTNanI9Y0QJWUBZN77AbXwSXrcbJ4pJZUKfbxqxSyFKz4ymeTfZhWYZ5ysb74f-vdPBt_vbnxEfXaB7vBUbO200xqBpwr_heJzcAE</recordid><startdate>19921005</startdate><enddate>19921005</enddate><creator>POLLARD, TD</creator><creator>GOLDBERG</creator><creator>SCHWARZ, WH</creator><general>American Society for Biochemistry and Molecular Biology</general><general>Amer Soc Biochemistry Molecular Biology Inc</general><scope>BLEPL</scope><scope>DTL</scope><scope>EZCTM</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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19921005</creationdate><title>Nucleotide exchange, structure, and mechanical properties of filaments assembled from ATP-actin and ADP-actin</title><author>POLLARD, TD ; GOLDBERG ; SCHWARZ, WH</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-201592c6a7dd656a0945d1ac53280de373a0075c19c43ceab4f9a78ac68fcf233</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>actin</topic><topic>Actin Cytoskeleton - chemistry</topic><topic>Actin Cytoskeleton - ultrastructure</topic><topic>Actins - chemistry</topic><topic>Adenosine Diphosphate - analogs & derivatives</topic><topic>Adenosine Diphosphate - chemistry</topic><topic>Adenosine Triphosphate - analogs & derivatives</topic><topic>Adenosine Triphosphate - chemistry</topic><topic>ADP</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>ATP</topic><topic>binding</topic><topic>Biochemistry & Molecular Biology</topic><topic>Biological and medical sciences</topic><topic>Biomechanical Phenomena</topic><topic>Biopolymers</topic><topic>Contractile proteins</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Holoproteins</topic><topic>Kinetics</topic><topic>Life Sciences & Biomedicine</topic><topic>Microscopy, Electron</topic><topic>Muscles - chemistry</topic><topic>Nucleotides - chemistry</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Science & Technology</topic><topic>skeletal muscle</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>POLLARD, TD</creatorcontrib><creatorcontrib>GOLDBERG</creatorcontrib><creatorcontrib>SCHWARZ, WH</creatorcontrib><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 1992</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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering 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>POLLARD, TD</au><au>GOLDBERG</au><au>SCHWARZ, WH</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nucleotide exchange, structure, and mechanical properties of filaments assembled from ATP-actin and ADP-actin</atitle><jtitle>The Journal of biological chemistry</jtitle><stitle>J BIOL CHEM</stitle><addtitle>J Biol Chem</addtitle><date>1992-10-05</date><risdate>1992</risdate><volume>267</volume><issue>28</issue><spage>20339</spage><epage>20345</epage><pages>20339-20345</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Actin monomers with bound ATP, ADP, or fluorescent analogues of these nucleotides exchange the nucleotide on a second time
scale, whereas filaments assembled from each of these species exchange their nucleotide with the solution at least 1,000 times
slower than monomers. Filaments assembled from either ATP-actin or ADP-actin are indistinguishable by electron microscopy
after negative staining. The dynamic elasticity and viscosity of filaments assembled from ATP-actin or ADP-actin or mixtures
of these two species are the same over a wide range of frequencies. These observations do not support a recent suggestion
(Janmey, P. A., Hvidt, S., Oster, G. F., Lamb, J., Stossel, T. P., and Hartwig, J. H. (1990) Nature 347, 95-99) that ATP hydrolysis
within actin filaments stiffens the polymer and alters both their structure and affinity for nucleotides. The difference in
observations between these two studies may be related to time-dependent changes in ADP-actin prepared in slightly different
ways.</abstract><cop>BETHESDA</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1400353</pmid><doi>10.1016/s0021-9258(19)88707-0</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | Web of Science - Science Citation Index Expanded - 1992<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" />; MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | actin Actin Cytoskeleton - chemistry Actin Cytoskeleton - ultrastructure Actins - chemistry Adenosine Diphosphate - analogs & derivatives Adenosine Diphosphate - chemistry Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - chemistry ADP Analytical, structural and metabolic biochemistry Animals ATP binding Biochemistry & Molecular Biology Biological and medical sciences Biomechanical Phenomena Biopolymers Contractile proteins Fundamental and applied biological sciences. Psychology Holoproteins Kinetics Life Sciences & Biomedicine Microscopy, Electron Muscles - chemistry Nucleotides - chemistry Proteins Rabbits Science & Technology skeletal muscle |
| title | Nucleotide exchange, structure, and mechanical properties of filaments assembled from ATP-actin and ADP-actin |
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