Dynamic Instability in a DNA-Segregating Prokaryotic Actin Homolog
Dynamic instability-the switching of a two-state polymer between phases of steady elongation and rapid shortening-is essential to the cellular function of eukaryotic microtubules, especially during chromosome segregation. Since the discovery of dynamic instability 20 years ago, no other biological p...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2004-11, Vol.306 (5698), p.1021-1025 |
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| creator | Garner, Ethan C. Campbell, Christopher S. Mullins, R. Dyche |
| description | Dynamic instability-the switching of a two-state polymer between phases of steady elongation and rapid shortening-is essential to the cellular function of eukaryotic microtubules, especially during chromosome segregation. Since the discovery of dynamic instability 20 years ago, no other biological polymer has been found to exhibit this behavior. Using total internal reflection fluorescence microscopy and fluorescence resonance energy transfer, we observe that the prokaryotic actin homolog ParM, whose assembly is required for the segregation of large, low-copy number plasmids, displays both dynamic instability and symmetrical, bidirectional polymerization. The dynamic instability of ParM is regulated by adenosine triphosphate (ATP) hydrolysis, and filaments are stabilized by a cap of ATP-bound monomers. ParM is not related to tubulin, so its dynamic instability must have arisen by convergent evolution driven by a set of common constraints on polymer-based segregation of DNA. |
| doi_str_mv | 10.1126/science.1101313 |
| format | Article |
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Dyche</creator><creatorcontrib>Garner, Ethan C. ; Campbell, Christopher S. ; Mullins, R. Dyche</creatorcontrib><description>Dynamic instability-the switching of a two-state polymer between phases of steady elongation and rapid shortening-is essential to the cellular function of eukaryotic microtubules, especially during chromosome segregation. Since the discovery of dynamic instability 20 years ago, no other biological polymer has been found to exhibit this behavior. Using total internal reflection fluorescence microscopy and fluorescence resonance energy transfer, we observe that the prokaryotic actin homolog ParM, whose assembly is required for the segregation of large, low-copy number plasmids, displays both dynamic instability and symmetrical, bidirectional polymerization. The dynamic instability of ParM is regulated by adenosine triphosphate (ATP) hydrolysis, and filaments are stabilized by a cap of ATP-bound monomers. ParM is not related to tubulin, so its dynamic instability must have arisen by convergent evolution driven by a set of common constraints on polymer-based segregation of DNA.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1101313</identifier><identifier>PMID: 15528442</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>Actin ; Actins ; Actins - chemistry ; Adenosine Triphosphate - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - physiology ; Bacterial Proteins - ultrastructure ; Bacteriology ; Biological and medical sciences ; Biopolymers - chemistry ; Cellular biology ; Deoxyribonucleic acid ; DNA ; DNA, Bacterial - metabolism ; Fluorescence ; Fluorescence Resonance Energy Transfer ; Fundamental and applied biological sciences. Psychology ; Genetic aspects ; Hydrolysis ; Kinetics ; Microbiology ; Microscopy ; Microscopy, Fluorescence ; Miscellaneous ; Monomers ; Mutagenesis ; Nucleation ; Numbers ; Observation ; Plasmids ; Polymerization ; Polymers ; Prokaryotes</subject><ispartof>Science (American Association for the Advancement of Science), 2004-11, Vol.306 (5698), p.1021-1025</ispartof><rights>Copyright 2004 American Association for the Advancement of Science</rights><rights>2005 INIST-CNRS</rights><rights>COPYRIGHT 2004 American Association for the Advancement of Science</rights><rights>COPYRIGHT 2004 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Nov 5, 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c782t-13e2471e635970472369958466431a177a02a751f45043f8045856bfa757e5a43</citedby><cites>FETCH-LOGICAL-c782t-13e2471e635970472369958466431a177a02a751f45043f8045856bfa757e5a43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3839433$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3839433$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27903,27904,57994,58227</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16268259$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15528442$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Garner, Ethan C.</creatorcontrib><creatorcontrib>Campbell, Christopher S.</creatorcontrib><creatorcontrib>Mullins, R. Dyche</creatorcontrib><title>Dynamic Instability in a DNA-Segregating Prokaryotic Actin Homolog</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Dynamic instability-the switching of a two-state polymer between phases of steady elongation and rapid shortening-is essential to the cellular function of eukaryotic microtubules, especially during chromosome segregation. Since the discovery of dynamic instability 20 years ago, no other biological polymer has been found to exhibit this behavior. Using total internal reflection fluorescence microscopy and fluorescence resonance energy transfer, we observe that the prokaryotic actin homolog ParM, whose assembly is required for the segregation of large, low-copy number plasmids, displays both dynamic instability and symmetrical, bidirectional polymerization. The dynamic instability of ParM is regulated by adenosine triphosphate (ATP) hydrolysis, and filaments are stabilized by a cap of ATP-bound monomers. ParM is not related to tubulin, so its dynamic instability must have arisen by convergent evolution driven by a set of common constraints on polymer-based segregation of DNA.</description><subject>Actin</subject><subject>Actins</subject><subject>Actins - chemistry</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - physiology</subject><subject>Bacterial Proteins - ultrastructure</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Biopolymers - chemistry</subject><subject>Cellular biology</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA, Bacterial - metabolism</subject><subject>Fluorescence</subject><subject>Fluorescence Resonance Energy Transfer</subject><subject>Fundamental and applied biological sciences. 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| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Actin Actins Actins - chemistry Adenosine Triphosphate - metabolism Bacterial Proteins - chemistry Bacterial Proteins - physiology Bacterial Proteins - ultrastructure Bacteriology Biological and medical sciences Biopolymers - chemistry Cellular biology Deoxyribonucleic acid DNA DNA, Bacterial - metabolism Fluorescence Fluorescence Resonance Energy Transfer Fundamental and applied biological sciences. Psychology Genetic aspects Hydrolysis Kinetics Microbiology Microscopy Microscopy, Fluorescence Miscellaneous Monomers Mutagenesis Nucleation Numbers Observation Plasmids Polymerization Polymers Prokaryotes |
| title | Dynamic Instability in a DNA-Segregating Prokaryotic Actin Homolog |
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