TCP1 complex is a molecular chaperone in tubulin biogenesis
- M. Yaffe, G. Farr, D. Miklos, A. Horwich, M. Sternlicht, H. Sternlicht
- BiologyNature
- 16 July 1992
It is concluded that TCP1 functions as a cytosolic chaperone in the biogenesis of tubulin, and newly translated tubulin subunits entered a 900K complex in a protease-sensitive conformation.
The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.
- H. Sternlicht, G. Farr, M. Sternlicht, J. Driscoll, K. Willison, M. Yaffe
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 15 October 1993
These findings demonstrate that there is a cytosolic pathway for folding tubulin and actin in vivo that involves the TCP1 complex and could be immunoprecipitated by using an anti-TCP1 antibody.
Structure-activity study of the inhibition of microtubule assembly in vitro by podophyllotoxin and its congeners.
- J. Loike, C. Brewer, H. Sternlicht, W. J. Gensler, S. Horwitz
- Chemistry, BiologyCancer Research
- 1 September 1978
Results suggest that rings C and D of these drugs are involved in their interaction with the podophyllotoxin-binding site in tubulin.
Conformational analysis of podophyllotoxin and its congeners. Structure--activity relationship in microtubule assembly.
- C. Brewer, J. Loike, S. Horwitz, H. Sternlicht, W. Gensler
- ChemistryJournal of Medicinal Chemistry
- 1 February 1979
Newly-synthesized beta-tubulin demonstrates domain-specific interactions with the cytosolic chaperonin.
- J. K. Dobrzynski, M. Sternlicht, G. Farr, H. Sternlicht
- Biology, ChemistryBiochemistry
- 10 December 1996
It is proposed that N- and C-terminal regions of beta-tubulin structurally interact with TRiC-binding region approximately 150-350 to inhibit binding to TRiB and thereby support the concept of quasi-native chaperonin-bound intermediates.
Alpha-tubulin influences nucleotide binding to beta-tubulin: an assay using picomoles of unpurified protein.
- G. Farr, M. Yaffe, H. Sternlicht
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 1 July 1990
The results demonstrate that the newly synthesized beta subunit and the heterodimer bind nucleotides with similar specificity, and nucleotide binding to the E site in the heterODimer may not be solely defined by thebeta subunit.
Colchicine inhibition of microtubule assembly via copolymer formation.
- H. Sternlicht, I. Ringel
- BiologyJournal of Biological Chemistry
- 25 October 1979
It is found that CD inhibited assembly by a mechanism which preserved the ability of microtubule ends to add tubulin, inconsistent with the end-poisoning model which recently was proposed as a general mechanism for assembly inhibition by CD.
Microtubule assembly is dependent on a cluster of basic residues in alpha-tubulin.
- J. Szasz, M. Yaffe, M. Elzinga, G. Blank, H. Sternlicht
- Biology, ChemistryBiochemistry
- 12 August 1986
This study demonstrates that the HRL in bovine brain tubulin is Lys-394, a residue proximal in the alpha-tubulin sequence to the highly negatively charged carboxy-terminus region (residues 412-450) previously implicated in assembly, and proposes on the basis of secondary structure considerations and published sequence data that Lys-393 is part of an evolutionarily conserved cluster of basic residues composed of Lys-395, His-393, and Arg-390.
Expression of a human alpha-tubulin: properties of the isolated subunit.
- M. Yaffe, B. Levison, J. Szasz, H. Sternlicht
- Biology, ChemistryBiochemistry
- 22 March 1988
It is suggested that the amino-terminal methionine of alpha-tubulin plays an essential role in the isolated subunit and/or in the heterodimer, a hypothesis supported by chemical reactivity studies.
Studies of macromolecular structure by 13 C nuclear magnetic resonance. II. A specific labeling approach to the study of histidine residues in proteins.
- D. T. Browne, G. L. Kenyon, E. Packer, H. Sternlicht, D. Wilson
- ChemistryJournal of the American Chemical Society
- 21 February 1973
...
...