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PMID: 270679 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Interactions of a photoaffinity analog of GTP with the proteins of microtubules.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 74 ·No. 10 ·1977-10-00 ·Pages 4375-7

Geahlen RL, Haley BE

Abstract

Tubulin dimers isolated from brain contain two GTP binding sites, a nonexchangeable site and an exchangeable site. To localize the exchangeable site, we used a photoaffinity analog of GTP, 8-azidoguanosine triphosphate (8-N3GTP), which supports tubulin polymerization in the absence of activating light. Photolysis of tubulin polymerized in the presence of 0.01 to 0.1 mM [beta, gamma-32P]8-N3GTP resulted in covalent incorporation of radioactivity only onto the beta monomer. Photolysis with 8-N3GTP also prevented any further repolymerization of the tubulin whereas like treatment in the presence of GTP had no effect. Preincubation of tubulin with GTP prevented photo-incorporation of [beta, gamma-32P]8-N3GTP whereas preincubation with ATP did not.

MeSH Terms

Binding Sites Glycoproteins/metabolism Guanosine Triphosphate/analogs & derivatives,metabolism,radiation effects Light Photolysis Protein Binding Tubulin/metabolism,radiation effects

Chemicals

Glycoproteins Tubulin Guanosine Triphosphate

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Geahlen R L

Haley B E

References (13)

13 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.74.10.4375

Published

1977-10-00

Pages

4375-7

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC431944

Subset

External Links

PubMed source DOI: 10.1073/pnas.74.10.4375 PMC Full Text View journal details

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Interactions of a photoaffinity analog of GTP with the proteins of microtubules.

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