PMID: 6403030Jan 4, 1983Paper

Tubulin-zinc interactions: binding and polymerization studies

Biochemistry
G R EagleR H Himes

Abstract

The binding of Zn2+ to tubulin and the ability of this cation to promote the polymorphic assembly of the protein were examined. Equilibrium binding showed the existence of more than 60 potential Zn2+ binding sites on the dimer, including a number of high-affinity sites. The number of high-affinity sites, estimated by using a standard amount of phosphocellulose to remove more weakly bound Zn2+, reached a maximum of 6-7.5 with increasing levels of Zn2+ in the incubation solution. The number also increased with time of incubation at a single Zn2+ concentration. It is suggested that tubulin is slowly denatured in the presence of Zn2+, exposing more binding sites. Cu+ and Cd2+ were effective inhibitors of Zn2+ binding; Mg2+, Mn2+, and Co2+ were much less effective, and Ca2+ was without effect. Zn2+ does not replace the tightly bound Mg2+. GTP reduces the amount of Zn2+ binding under equilibrium conditions and the amount bound to high-affinity sites. Zinc-induced protofilament sheets are produced at a Zn2+/tubulin ratio of 5 in the presence of 0.5 mM GTP, conditions where about two to three Zn2+ ions would be bound to the dimer. At higher GTP concentrations, less assembly occurred, and the products were narrower sheets and microtubul...Continue Reading

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Citations

Jan 1, 1993·Cell Motility and the Cytoskeleton·S LobertJ J Correia
Jul 15, 1994·Experientia·R S Bedwal, A Bahuguna
Jan 1, 1990·Biological Trace Element Research·P I OteizaC L Keen
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Oct 12, 2013·ACS Chemical Biology·Nicholas J Pace, Eranthie Weerapana
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Jan 1, 1987·Cell Motility and the Cytoskeleton·E A WhiteR H Himes
Jan 1, 1997·Neurobiology of Disease·M P Cuajungco, G J Lees
Feb 26, 2014·Communicative & Integrative Biology·Winyoo ChowanadisaiMark A Messerli
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Mar 7, 2021·Biomedicines·Math P CuajungcoMarcelo E Tolmasky
Jan 8, 2019·ACS Omega·Zachary J DonhauserEvan C Sheffield

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