PROHEAD AND DNA-GP3-DEPENDENT ATPASE ACTIVITY OF THE DNA PACKAGING PROTEIN GP16 OF BACTERIOPHAGE-PHI-29
PROHEAD AND DNA-GP3-DEPENDENT ATPASE ACTIVITY OF THE DNA PACKAGING PROTEIN GP16 OF BACTERIOPHAGE-PHI-29
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DOI:
10.1016/0022-2836(87)90121-5
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发表时间:
1987-09-20
影响因子:
5.6
通讯作者:
ANDERSON, D
中科院分区:
文献类型:
--
作者:
GUO, PX;PETERSON, C;ANDERSON, D
The ATPase activity of the DNA packaging protein gp16 (gene product 16) of bacteriophage .vphi.29 was studied in the completely defined in-vitro assembly system. ATP was hydrolyzed to ADP and Pi in the packaging reaction that included purified proheads, DNA-gp3 and gp16. Approximately one molecule of ATP was used in the packaging of 2 base-pairs of .vphi. DNA, or 9 .times. 103 ATP molecules per virion. The hydrolysis of ATP by gp16 was both prohead and DNA-gp3 dependent. gp16 contained both the "A-type" and the "B-type" ATP-binding consensus sequences (Walker et al., 1982) and the predicted secondary structure for ATP binding. The A-type sequence of gp16 was "basic-hydrophobic region-G-X2-G-X-G-K-S-X7-hydrophobic", and similar sequences were found in the phage DNA packaging proteins gpA of lambda, gp19 of T7 and gp17 of T4. Having both the ATP-binding and potential magnesium-binding domains, all of these proteins probably function as ATPases and may have common prohead-binding capabilities. The .vphi. protein gp3, covalently bound to the DNA, may be analogous in function to proteins gpNu1 of lambda and gp1 of .vphi.21 that bind the DNA.