Microtubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton.

Microtubules play crucial roles in cytokinesis, transport, and motility, and are therefore superb targets for anti-cancer drugs. All tubulins evolved from a common ancestor they share with the distantly related bacterial cell division protein FtsZ, but while eukaryotic tubulins evolved into highly c...

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Autores principales: Martin Pilhofer, Mark S Ladinsky, Alasdair W McDowall, Giulio Petroni, Grant J Jensen
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Publicado: Public Library of Science (PLoS) 2011
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Acceso en línea:https://doaj.org/article/f141329f0fcb416fa651af25ac7a8509
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spelling oai:doaj.org-article:f141329f0fcb416fa651af25ac7a85092021-11-18T05:36:51ZMicrotubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton.1544-91731545-788510.1371/journal.pbio.1001213https://doaj.org/article/f141329f0fcb416fa651af25ac7a85092011-12-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22162949/?tool=EBIhttps://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Microtubules play crucial roles in cytokinesis, transport, and motility, and are therefore superb targets for anti-cancer drugs. All tubulins evolved from a common ancestor they share with the distantly related bacterial cell division protein FtsZ, but while eukaryotic tubulins evolved into highly conserved microtubule-forming heterodimers, bacterial FtsZ presumably continued to function as single homopolymeric protofilaments as it does today. Microtubules have not previously been found in bacteria, and we lack insight into their evolution from the tubulin/FtsZ ancestor. Using electron cryomicroscopy, here we show that the tubulin homologs BtubA and BtubB form microtubules in bacteria and suggest these be referred to as "bacterial microtubules" (bMTs). bMTs share important features with their eukaryotic counterparts, such as straight protofilaments and similar protofilament interactions. bMTs are composed of only five protofilaments, however, instead of the 13 typical in eukaryotes. These and other results suggest that rather than being derived from modern eukaryotic tubulin, BtubA and BtubB arose from early tubulin intermediates that formed small microtubules. Since we show that bacterial microtubules can be produced in abundance in vitro without chaperones, they should be useful tools for tubulin research and drug screening.Martin PilhoferMark S LadinskyAlasdair W McDowallGiulio PetroniGrant J JensenPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 9, Iss 12, p e1001213 (2011)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Martin Pilhofer
Mark S Ladinsky
Alasdair W McDowall
Giulio Petroni
Grant J Jensen
Microtubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton.
description Microtubules play crucial roles in cytokinesis, transport, and motility, and are therefore superb targets for anti-cancer drugs. All tubulins evolved from a common ancestor they share with the distantly related bacterial cell division protein FtsZ, but while eukaryotic tubulins evolved into highly conserved microtubule-forming heterodimers, bacterial FtsZ presumably continued to function as single homopolymeric protofilaments as it does today. Microtubules have not previously been found in bacteria, and we lack insight into their evolution from the tubulin/FtsZ ancestor. Using electron cryomicroscopy, here we show that the tubulin homologs BtubA and BtubB form microtubules in bacteria and suggest these be referred to as "bacterial microtubules" (bMTs). bMTs share important features with their eukaryotic counterparts, such as straight protofilaments and similar protofilament interactions. bMTs are composed of only five protofilaments, however, instead of the 13 typical in eukaryotes. These and other results suggest that rather than being derived from modern eukaryotic tubulin, BtubA and BtubB arose from early tubulin intermediates that formed small microtubules. Since we show that bacterial microtubules can be produced in abundance in vitro without chaperones, they should be useful tools for tubulin research and drug screening.
format article
author Martin Pilhofer
Mark S Ladinsky
Alasdair W McDowall
Giulio Petroni
Grant J Jensen
author_facet Martin Pilhofer
Mark S Ladinsky
Alasdair W McDowall
Giulio Petroni
Grant J Jensen
author_sort Martin Pilhofer
title Microtubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton.
title_short Microtubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton.
title_full Microtubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton.
title_fullStr Microtubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton.
title_full_unstemmed Microtubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton.
title_sort microtubules in bacteria: ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton.
publisher Public Library of Science (PLoS)
publishDate 2011
url https://doaj.org/article/f141329f0fcb416fa651af25ac7a8509
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