Articles written in Journal of Biosciences
Volume 5 Issue 3 September 1983 pp 203-208
In this communication, we report the presence of a unique colchicine-binding activity in the polysomes of rat brain. This drug-binding property, is somewhat similar to that of tubulin isolated from many sources; however, it differs in several bio-chemical characteristics such as (i) thermal stability of colchicine-binding site, (ii) protection of binding site by vinblastine and (iii) time required for binding equilibration. Such binding of colchicine to the polysomes is most probably due to the presence of a nascent peptide chain of tubulin in the polysome.
Volume 6 Issue 4 October 1984 pp 431-457
Microtubules are ubiquitous cellular structures found in eukaryotic organisms and responsible for a variety of functions. These functions include mitosis, motility, cytoskeletal architecture, intracellular transport and secretion. The major structural component of microtubules is tubulin, a dimeric protein molecule consisting of two similar but nonidentical subunits (α and β) each of about molecular weight 55,000. With the introduction of radioactive colchicine for the first time it has been reported that colchicine binds specifically to tubulin. At this point microtubule research stepped up to a new era linking microtubules with other spindle poisons which are structurally diverse as well as binding at different sites on to the tubulin heterodimer. These antimicrotubular agents have already provided valuable information regarding microtubule-mediated cellular functions and its association and dissociation phenomena. Tubulins appear to be conserved proteins based on
Volume 11 Issue 1-4 March 1987 pp 525-536
Colchicine-tubulin dimer comPlex, a Potent inhibitor of normal microtubule assembly undergoes extensive self-assembly in the Presence of 1 X 10-4 M zinc sulPhate. Polymers assembled from colchicine-tubulin dimer comPlexes are sensitive to cold.
Although colchicine can be accomodated within the Polymeric structure, the drug cannot bind to tubulin subunits in the intact Polymers. This is evidenced by the fact that (a) the colchicine binding activity of tubulin is lost when allowed to Polymerize with zinc sulPhate, (b) the loss in colchicine binding could be Prevented by Preincubation of tubulin with 1 X 10-3 M CaCl2 or 1 X 10-5 M vinblastine sulPhate and finally (c) no loss in colchicine binding activity is found when tubulin is kePt at a concentration far below the critical concentration for Polymerization. Unlike colchicine, its B-ring analogues desacetamido colchicine (devoid of the B-ring subtituent) and 2-methoxy-5-(2′, 3′, 4′-trimethoxyPhenyl) troPone (devoid of the B-ring) can bind to tubulin subunits in the intact Polymers.
Thus we conclude that the colchicine binding domain on the tubulin molecule is mostly (if not comPletely) exPosed in the Zn(II) -induced Polymers and the B-ring substituent Plays a major role in determining the binding ability of a colchicine analogue to tubulin in the intact Zn(II) -induced sheets.
Volume 24 Issue S1 March 1999 pp 5-31
F Parak A Ostermann G U Nienhaus Nobuo Niimura William A Eaton Stephen J Hagen Eric R Henry James Hofrichter Gouri Jas Lisa Lapidus Victor Muñoz Chih-chen Wang Abani Bhuyan Javant Udgaonkar Heinz Rüterians Derek N Woolfson M D Finucane J H Lees M J Pandya G Spooner M Tuna Wilma K Olson K V R Chary E Westhof I G Wool C C Correll V I Ivanov S A Bondarenko E M Zdobnov A D Beniaminov E E Minyat N B Ulyanov Dale B Wigley Nobuo Shimamoto Takashi Kinebuchi Hiroyuki Kabata Osamu Kurosawa Masao Washizu Barbara Baird David Holowka H Belrhali P Nollert A Royant J P Rosenbusch E M Landau E Pebav-Peyroula Anil K Lala Patrick R D’Silva Daniela Pietrobon Paolo Pinton Paulo Magalhaes Anna Chiesa Marisa Brini Tullio Pozzan Rosario Rizzuto M Montai Shu-Rong Wang José L Carrascosa B Bhattacharyya Ian A Wilson Dinakar M Salunke Kurt Drickamer Anne Imberty A Surolia Louise N Johnson Michal Neeman S M Prince K McLuskey R J Cogdell K McAuley N W Isaacs G Venturoli F Drepper J C Williams J P Allen X Lin P Mathis R van Grondelle Wolfgang Junge T Tsukihara K Shinzawa-Itoh R Nakashima E Yamashita M J Fei N Inoue T Tomizaki C Peters Libeu S Yoshikawa Patrick Chaussepied Keiichi Namba Marie-France Carlier Fariza Ressacl Valerie Laurent Thomas Loisel Coumaran Egile Philippe Sansonetti Dominique Pantaloni Manju Bansal E W Knapp M G Ullmann A Amadei B L de Groot M A Ceruso M Paci H J C Berendsen A Di Nola V Di Francesco P J Munson J Garnier Sung-Hou Kim Jean-Michel Claverie Ian C P Smith P T Callaghan Bruce Cornell Ratna S Phadke Kazuhiko Kinosita D Goldfarb I Qromov C Shutter I Pecht P Manikandan R Carmieli T Shane David S Moss Clare E Sansom Jeremy K Cockcroft Ian J Tickle Huub C P Driessen J Raul Grigera Ramen K Poddar Charles R Cantor Barry Robson Jean Garnier John Helliwell Sunney I Chan Ronald Rock
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