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Activation of recA protein: the pitch of the helical complex with single-stranded DNA

Hewat, E.A.; Ruigrok, R.W.; DiCapua, E.

EMBO Journal 10(9): 2695-2698

1991

ISSN/ISBN: 0261-4189
PMID: 1868839
Document Number: 378791
The complex of recA protein with single-stranded DNA in the presence of ATP is the active species in the three enzymatic activities of recA: the initiation of strand exchange, the hydrolysis of ATP and the cleavage of repressors. Here we find by cryo-electron microscopy of unstained and unfixed samples that the helical structure of the protein coat in this complex differs slightly but significantly from the structure in the complex with double-stranded DNA. We discuss how the larger pitch of the complex with single strands (100 +/- 2 A compared with 95 +/- 2 A with double strands) could contribute to its higher enzymatic activity.

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