| Autor: |
Logan KM; Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, Massachusetts 01655-0103, USA., Forget AL, Verderese JP, Knight KL |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry [Biochemistry] 2001 Sep 25; Vol. 40 (38), pp. 11382-9. |
| DOI: |
10.1021/bi011081u |
| Abstrakt: |
RecA protein undergoes ATP- and DNA-induced conformational changes that result in different helical parameters for free protein filaments versus RecA/ATP/DNA nucleoprotein filaments. Previous mutational studies of a particular region of the RecA oligomeric interface suggested that cross-subunit contacts made by residues K6 and R28 were more important for stabilization of free protein oligomers than nucleoprotein filaments [Eldin, S., et al. (2000) J. Mol. Biol. 299, 91-101]. Using mutant proteins with specifically engineered Cys substitutions, we show here that the efficiency of cross-subunit disulfide bond formation at certain positions in this region changes in the presence of ATP or ATP/DNA. Our results support the idea that specific cross-subunit interactions that occur within this region of the subunit interface are different in free RecA protein versus RecA/ATP/DNA nucleoprotein filaments. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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