| Autor: |
Ruigrok, R.W., Bohrmann, B., Hewat, E., Engel, A., Kellenberger, E., DiCapua, E. |
| Zdroj: |
The EMBO Journal; January 1993, Vol. 12 Issue: 1 p9-16, 8p |
| Abstrakt: |
When recA protein is enzymatically inactive in vitro, it adopts a more compact helical polymer form than that of the active protein polymerized onto DNA in the presence of ATP. Here we describe some aspects of this structure. By cryo‐electron microscopy, a pitch of 76 A is found for both the self‐polymer and the inactive complex with ssDNA. A smaller pitch of 64 A is observed in conventional electron micrographs. The contour length of complexes with ssDNA was used to estimate the binding stoichiometry in the compact complex, 6 +/− 1 nt/recA. In addition, the compact structure was observed in vivo in Escherichia coli: inclusion bodies produced upon induction of recA expression in an overproducing strain have a fibrous morphology with the structural parameters of the compact polymer. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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