F-actin is intermolecularly crosslinked by N,N'-p-phenylenedimaleimide through lysine-191 and cysteine-374.
AUTOR(ES)
Elzinga, M
RESUMO
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 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=391977Documentos Relacionados
- Heterotrimeric G proteins in synaptoneurosome membranes are crosslinked by p-phenylenedimaleimide, yielding structures comparable in size to crosslinked tubulin and F-actin.
- F-actin in conifer roots
- Relating microstructure to rheology of a bundled and cross-linked F-actin network in vitro
- Organized F-actin is essential for normal trichome morphogenesis in Arabidopsis.
- Fimbrin is a cytoskeletal protein that crosslinks F-actin in vitro.
