Nucleotide specificity in microtubule assembly in vitro
A procedure is described for removing most of the GDP bound at the exchangeable GTP binding site (E site) of tubulin. Microtubule protein containing substoichiometric amounts of GDP at the E site is found to polymerize in response to: (a) two nonhydrolyzable ATP analogues, adenylyl imidodiphosphate...
Gespeichert in:
Veröffentlicht in: | Biochemistry (Easton) 1978-02, Vol.17 (4), p.734-740 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 740 |
---|---|
container_issue | 4 |
container_start_page | 734 |
container_title | Biochemistry (Easton) |
container_volume | 17 |
creator | Penningroth, Stephen M Kirschner, Marc W |
description | A procedure is described for removing most of the GDP bound at the exchangeable GTP binding site (E site) of tubulin. Microtubule protein containing substoichiometric amounts of GDP at the E site is found to polymerize in response to: (a) two nonhydrolyzable ATP analogues, adenylyl imidodiphosphate (AMP-PNP) and adenylyl beta, gamma-methylenediphosphonate (AMP-PCP); and (b) substoichiometric levels of GTP or dGTP. The results are interpreted as suggesting that: (1) when GDP is removed from tubulin, the E site shows broad specificity for nucleoside triphosphates: (2) microtubule assembly can be induced by the binding of substoichiometric amounts of nucleoside triphosphate to the E site. |
doi_str_mv | 10.1021/bi00597a028 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_83835592</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>83835592</sourcerecordid><originalsourceid>FETCH-LOGICAL-a268t-d241af4acfecaf51d9a81a02767d3d7a717c39a76669e99d68a7c9191466f8153</originalsourceid><addsrcrecordid>eNptkL1PwzAQxS3EVylMrAyZYEAB24nteESF8qEKUCkLi3VxHMklaYqdIPrfY0hVMTCd7t5P754eQscEXxBMyWVuMWZSAKbZFhoQRnGcSsm20QBjzGMqOd5HB97Pw5pike6hXU4TkdIBEo-drkzT2sJEfmm0La227Sqyi6i22jVtl3eVicB7U-fV7_3Ttq45RDslVN4crecQvY5vZqO7ePJ0ez-6msRAedbGBU0JlCno0mgoGSkkZCTkFFwUSSFAEKETCYJzLo2UBc9AaEkkSTkvM8KSITrtfZeu-eiMb1VtvTZVBQvTdF5lSZYwJmkAz3swhPbemVItna3BrRTB6qcl9aelQJ-sbbu8NsWG7WsJctzL1rfma6OCe1dcJIKp2fOLepvKBzy-nqpx4M96HrRX86Zzi9DJv4-_AWbgfR4</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>83835592</pqid></control><display><type>article</type><title>Nucleotide specificity in microtubule assembly in vitro</title><source>MEDLINE</source><source>ACS Publications</source><creator>Penningroth, Stephen M ; Kirschner, Marc W</creator><creatorcontrib>Penningroth, Stephen M ; Kirschner, Marc W</creatorcontrib><description>A procedure is described for removing most of the GDP bound at the exchangeable GTP binding site (E site) of tubulin. Microtubule protein containing substoichiometric amounts of GDP at the E site is found to polymerize in response to: (a) two nonhydrolyzable ATP analogues, adenylyl imidodiphosphate (AMP-PNP) and adenylyl beta, gamma-methylenediphosphonate (AMP-PCP); and (b) substoichiometric levels of GTP or dGTP. The results are interpreted as suggesting that: (1) when GDP is removed from tubulin, the E site shows broad specificity for nucleoside triphosphates: (2) microtubule assembly can be induced by the binding of substoichiometric amounts of nucleoside triphosphate to the E site.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00597a028</identifier><identifier>PMID: 623742</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Adenosine Triphosphate - analogs & derivatives ; Animals ; Brain ; Glycoproteins ; Guanosine Diphosphate ; Guanosine Triphosphate ; Kinetics ; Microtubules - ultrastructure ; Nerve Tissue Proteins ; Protein Binding ; Swine ; Tubulin</subject><ispartof>Biochemistry (Easton), 1978-02, Vol.17 (4), p.734-740</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a268t-d241af4acfecaf51d9a81a02767d3d7a717c39a76669e99d68a7c9191466f8153</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00597a028$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00597a028$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2763,27075,27923,27924,56737,56787</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/623742$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Penningroth, Stephen M</creatorcontrib><creatorcontrib>Kirschner, Marc W</creatorcontrib><title>Nucleotide specificity in microtubule assembly in vitro</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>A procedure is described for removing most of the GDP bound at the exchangeable GTP binding site (E site) of tubulin. Microtubule protein containing substoichiometric amounts of GDP at the E site is found to polymerize in response to: (a) two nonhydrolyzable ATP analogues, adenylyl imidodiphosphate (AMP-PNP) and adenylyl beta, gamma-methylenediphosphonate (AMP-PCP); and (b) substoichiometric levels of GTP or dGTP. The results are interpreted as suggesting that: (1) when GDP is removed from tubulin, the E site shows broad specificity for nucleoside triphosphates: (2) microtubule assembly can be induced by the binding of substoichiometric amounts of nucleoside triphosphate to the E site.</description><subject>Adenosine Triphosphate - analogs & derivatives</subject><subject>Animals</subject><subject>Brain</subject><subject>Glycoproteins</subject><subject>Guanosine Diphosphate</subject><subject>Guanosine Triphosphate</subject><subject>Kinetics</subject><subject>Microtubules - ultrastructure</subject><subject>Nerve Tissue Proteins</subject><subject>Protein Binding</subject><subject>Swine</subject><subject>Tubulin</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkL1PwzAQxS3EVylMrAyZYEAB24nteESF8qEKUCkLi3VxHMklaYqdIPrfY0hVMTCd7t5P754eQscEXxBMyWVuMWZSAKbZFhoQRnGcSsm20QBjzGMqOd5HB97Pw5pike6hXU4TkdIBEo-drkzT2sJEfmm0La227Sqyi6i22jVtl3eVicB7U-fV7_3Ttq45RDslVN4crecQvY5vZqO7ePJ0ez-6msRAedbGBU0JlCno0mgoGSkkZCTkFFwUSSFAEKETCYJzLo2UBc9AaEkkSTkvM8KSITrtfZeu-eiMb1VtvTZVBQvTdF5lSZYwJmkAz3swhPbemVItna3BrRTB6qcl9aelQJ-sbbu8NsWG7WsJctzL1rfma6OCe1dcJIKp2fOLepvKBzy-nqpx4M96HrRX86Zzi9DJv4-_AWbgfR4</recordid><startdate>19780221</startdate><enddate>19780221</enddate><creator>Penningroth, Stephen M</creator><creator>Kirschner, Marc W</creator><general>American Chemical Society</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>19780221</creationdate><title>Nucleotide specificity in microtubule assembly in vitro</title><author>Penningroth, Stephen M ; Kirschner, Marc W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a268t-d241af4acfecaf51d9a81a02767d3d7a717c39a76669e99d68a7c9191466f8153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Adenosine Triphosphate - analogs & derivatives</topic><topic>Animals</topic><topic>Brain</topic><topic>Glycoproteins</topic><topic>Guanosine Diphosphate</topic><topic>Guanosine Triphosphate</topic><topic>Kinetics</topic><topic>Microtubules - ultrastructure</topic><topic>Nerve Tissue Proteins</topic><topic>Protein Binding</topic><topic>Swine</topic><topic>Tubulin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Penningroth, Stephen M</creatorcontrib><creatorcontrib>Kirschner, Marc W</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Penningroth, Stephen M</au><au>Kirschner, Marc W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nucleotide specificity in microtubule assembly in vitro</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1978-02-21</date><risdate>1978</risdate><volume>17</volume><issue>4</issue><spage>734</spage><epage>740</epage><pages>734-740</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>A procedure is described for removing most of the GDP bound at the exchangeable GTP binding site (E site) of tubulin. Microtubule protein containing substoichiometric amounts of GDP at the E site is found to polymerize in response to: (a) two nonhydrolyzable ATP analogues, adenylyl imidodiphosphate (AMP-PNP) and adenylyl beta, gamma-methylenediphosphonate (AMP-PCP); and (b) substoichiometric levels of GTP or dGTP. The results are interpreted as suggesting that: (1) when GDP is removed from tubulin, the E site shows broad specificity for nucleoside triphosphates: (2) microtubule assembly can be induced by the binding of substoichiometric amounts of nucleoside triphosphate to the E site.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>623742</pmid><doi>10.1021/bi00597a028</doi><tpages>7</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0006-2960 |
ispartof | Biochemistry (Easton), 1978-02, Vol.17 (4), p.734-740 |
issn | 0006-2960 1520-4995 |
language | eng |
recordid | cdi_proquest_miscellaneous_83835592 |
source | MEDLINE; ACS Publications |
subjects | Adenosine Triphosphate - analogs & derivatives Animals Brain Glycoproteins Guanosine Diphosphate Guanosine Triphosphate Kinetics Microtubules - ultrastructure Nerve Tissue Proteins Protein Binding Swine Tubulin |
title | Nucleotide specificity in microtubule assembly in vitro |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-12T09%3A08%3A44IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Nucleotide%20specificity%20in%20microtubule%20assembly%20in%20vitro&rft.jtitle=Biochemistry%20(Easton)&rft.au=Penningroth,%20Stephen%20M&rft.date=1978-02-21&rft.volume=17&rft.issue=4&rft.spage=734&rft.epage=740&rft.pages=734-740&rft.issn=0006-2960&rft.eissn=1520-4995&rft_id=info:doi/10.1021/bi00597a028&rft_dat=%3Cproquest_cross%3E83835592%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=83835592&rft_id=info:pmid/623742&rfr_iscdi=true |