F-actin is intermolecularly crosslinked by N,N'-p-phenylenedimaleimide through lysine-191 and cysteine-374.
- 1 November 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (21), 6599-6602
- https://doi.org/10.1073/pnas.81.21.6599
Abstract
The bifunctional reagent N,N''-p-phenylenedimaleimide (PDM) is being used in an attempt to measure distances between specific side chains in adjacent monomers within [rabbit muscle] F-actin. [14C]PDM was synthesized and was used to crosslink F-actin. Uncrosslinked actin was removed by gel filtration, and, from an arginine-specific tryptic digest of the covalently crosslinked dimers and higher oligomers, one radioactive crosslinked peptide was obtained in high yield. Amino acid composition and sequence analysis indicated that it comprises residues 184-196 of one monomer and 373-375 of an adjacent actin molecule, bridged by PDM through Cys-374 and Lys-191. Thus, these groups are shown to be 1.2-1.4 nm apart in adjacent actin monomers in F-actin. This information may be crucial in establishing the orientation of actin monomers within F-actin.This publication has 20 references indexed in Scilit:
- Actin-actin and actin-deoxyribonuclease I contact sites in the actin sequenceBiochemistry, 1984
- Identification of myosin-binding sites on the actin sequenceBiochemistry, 1982
- Change of reactivity of lysine residues upon actin polymerizationBiochemistry, 1981
- Structure of the actin–myosin interfaceNature, 1981
- Isolation and characterization of the trypsin‐modified myosin ‐S1 derivativesFEBS Letters, 1981
- Structure of crystalline actin sheetsNature, 1980
- Three-dimensional image reconstruction of actin-tropomyosin complex and actin-tropomyosin-troponin T-troponin I complexJournal of Molecular Biology, 1975
- Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filamentsJournal of Molecular Biology, 1970
- Cross-Linking of Bovine Pancreatic Ribonuclease A with Dimethyl Adipimidate*Biochemistry, 1967
- Tertiary Structure of RibonucleaseNature, 1967