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PMID: 1304380 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

The accessibility of etheno-nucleotides to collisional quenchers and the nucleotide cleft in G- and F-actin.

Protein science : a publication of the Protein Society ·Vol. 1 ·No. 8 ·1992-08-00 ·Pages 1014-22

Root DD, Reisler E

Abstract

Recent publication of the atomic structure of G-actin (Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F., & Holmes, K. C., 1990, Nature 347, 37-44) raises questions about how the conformation of actin changes upon its polymerization. In this work, the effects of various quenchers of etheno-nucleotides bound to G- and F-actin were examined in order to assess polymerization-related changes in the nucleotide phosphate site. The Mg(2+)-induced polymerization of actin quenched the fluorescence of the etheno-nucleotides by approximately 20% simultaneously with the increase in light scattering by actin. A conformational change at the nucleotide binding site was also indicated by greater accessibility of F-actin than G-actin to positively, negatively, and neutrally charged collisional quenchers. The difference in accessibility between G- and F-actin was greatest for I-, indicating that the environment of the etheno group is more positively charged in the polymerized form of actin. Based on calculations of the change in electric potential of the environment of the etheno group, specific polymerization-related movements of charged residues in the atomic structure of G-actin are suggested. The binding of S-1 to epsilon-ATP-G-actin increased the accessibility of the etheno group to I- even over that in Mg(2+)-polymerized actin. The quenching of the etheno group by nitromethane was, however, unaffected by the binding of S-1 to actin. Thus, the binding of S-1 induces conformational changes in the cleft region of actin that are different from those caused by Mg2+ polymerization of actin.(ABSTRACT TRUNCATED AT 250 WORDS)

MeSH Terms
Actins/chemistry,metabolism Adenosine Diphosphate/analogs & derivatives,metabolism Amino Acid Sequence Animals Binding Sites Ethenoadenosine Triphosphate/metabolism Fluorescent Dyes Kinetics Macromolecular Substances Magnesium/pharmacology Mathematics Methane/analogs & derivatives,pharmacology Muscles/metabolism Myosins/metabolism Nitroparaffins/pharmacology Potassium Iodide/pharmacology Protein Conformation Rabbits Spectrometry, Fluorescence Thallium/pharmacology
Chemicals
Actins Ethenoadenosine Triphosphate Fluorescent Dyes Macromolecular Substances Nitroparaffins Potassium Iodide thallium chloride 1,N(6)-ethenoadenosine diphosphate Adenosine Diphosphate Thallium Myosins Magnesium Methane nitromethane
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Root D D
Molecular Biology Institute, University of California, Los Angeles 90024.
Reisler E
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29 references, click to expand
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Article Info
Journal
Protein science : a publication of the Protein Society
Abbr.
Protein Sci
ISSN
0961-8368
Published
1992-08-00
Pages
1014-22
Language
English
Region
United States
NLM ID
9211750
PMCID
PMC2142168
Subset
IM
Grants
NIAMS NIH HHS · R01 AR022031 · United States
NIAMS NIH HHS · AR 2203 · United States
NCI NIH HHS · CA-9056 · United States
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