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• W2083643003 abstract "In the recently solved structure of TMR-modified ADP-G-actin, the nucleotide cleft is in a closed state conformation, and the D-loop contains an α-helix (L. R. Otterbein, P. Graceffa, and R. Dominguez, 2001, Science, 293:708–711). Subsequently, questions were raised regarding the possible role of the TMR label on Cys374 in determining these aspects of G-actin structure. We show here that the susceptibility of D-loop on G-actin to subtilisin cleavage, and ATP/ADP-dependent changes in this cleavage, are not affected by TMR-labeling of actin. The TMR modification inhibits nucleotide exchange, but has no effect on DNase I binding and the fast phase of tryptic digestion of actin. These results show an absence of allosteric effects of TMR on subdomain 2, while confirming ATP/ADP-dependent changes in D-loop structure. In conjunction with similar results obtained on actin-gelsolin segment 1 complex, this works reveals the limitations of solution methods in probing the putative open and closed nucleotide cleft states of G-actin." @default.
• W2083643003 created "2016-06-24" @default.
• W2083643003 creator A5004456531 @default.
• W2083643003 creator A5038398169 @default.
• W2083643003 date "2003-10-01" @default.
• W2083643003 modified "2023-09-25" @default.
• W2083643003 title "Solution Properties of Tetramethylrhodamine-Modified G-Actin" @default.
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• W2083643003 doi "https://doi.org/10.1016/s0006-3495(03)74669-4" @default.
• W2083643003 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1303470" @default.
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