期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 275, 期 45, 页码 35311-35319出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M004309200
关键词
-
The terminase of bacteriophage SPP1, constituted by a large (G2P) and a small (GIP) subunit, is essential for the initiation of DNA packaging. A hexa-histidine G2P (H6-G2P), which is functional in vivo, possesses endonuclease, ATPase, and double-stranded DNA binding activities. H6-G2P introduces a cut with preference at the 5'-RCGG down arrow CW-3' sequence. Distamycin A, which is a minor groove binder that mimics the architectural structure generated by G1P at pac, enhances the specific cut at both bona fide 5'-CTATTGCGG down arrow C-3' sequences within pacC of SPP1 and SF6 phages, H6-G2P hydrolyzes rATP or dATP to the corresponding rADP or dADP and Pi, H6-G2P interacts with two discrete G1P domains (I and II). Full-length GIP and G1P Delta N62 (lacking domain I) stimulate 3,5- and 1,9-fold, respectively, the ATPase activity of H6-G2P. The results presented suggest that a DNA structure, artificially promoted by distamycin A or facilitated by the assembly of GIP at pact and/or pacR, stimulates H6-G2P cleavage at both target sites within pacC. In the presence of two GIP decamers per H6-G2P monomer, the H6-G2P endonuclease is repressed, and the ATPase activity stimulated. Based on these results, we propose a model that can account for the role of terminase in headful packaging.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据