DNA-STIMULATED ATPASE ACTIVITY ON THE LON (CAPR) PROTEIN
DNA-STIMULATED ATPASE ACTIVITY ON THE LON (CAPR) PROTEIN
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DOI:
10.1128/jb.158.1.195-201.1984
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发表时间:
1984-01-01
影响因子:
3.2
通讯作者:
MARKOVITZ, A
中科院分区:
文献类型:
--
作者:
CHARETTE, MF;HENDERSON, GW;MARKOVITZ, A
The gene product of the pleiotropic lon (also called capR) locus in Escherichia coli, the CapR protein, is an ATP hydrolysis-dependent protease and a nonspecific nucleic acid-binding protein. It is also a DNA-stimulated ATPase. This new activity is distinct from the protease-associated ATPase activity and occurred in the absence of proteolytic substrate. The reaction required the presence of a divalent cation and had a pH optimum of 8.0. The products of the reaction were ADP and Pi. No adenylation or phosphorylation of the DNA or proteins was detected. The maximum rate of ATP hydrolysis occurred in the presence of supercoiled (form I) DNA. Relaxed circles (form II), double-stranded DNA and single-stranded DNA were less effective in promoting ATPase activity. RNA was inactive. The DNA-stimulated ATPase activity was inhibited by a mutationally altered form of the CapR protein called the CapR9 protein. The interaction of the CapR and CapR9 subunits suggests that this enzymatic activity of the CapR protein is oligomeric in the presence of DNA. These experiments indicate a possible role for nucleic acids in the regulation of all lon (capR) activity.