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Biochemical mechanism of the DNA pac...

Al-Zahrani, Abdulrahman S.

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Biochemical mechanism of the DNA packaging ATPase from bacteriophage T4.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Biochemical mechanism of the DNA packaging ATPase from bacteriophage T4./
作者:	Al-Zahrani, Abdulrahman S.
面頁冊數:	113 p.
附註:	Adviser: Venigalla B. Rao.
Contained By:	Dissertation Abstracts International67-04B.
標題:	Biology, Molecular. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3214662
ISBN:	9780542655777

Biochemical mechanism of the DNA packaging ATPase from bacteriophage T4.
Al-Zahrani, Abdulrahman S.

Biochemical mechanism of the DNA packaging ATPase from bacteriophage T4. - 113 p.

Adviser: Venigalla B. Rao.

Thesis (Ph.D.)--The Catholic University of America, 2006.

Terminases are enzymes common to many double-stranded DNA bacteriophages as well as eukaroytic DNA viruses. These enzymes excise a single viral genome from a concatemeric DNA precursor and package it into a preformed protective capsid by ATP hydrolysis. T4 terminase complex is comprised of the large subunit gp17 and the small subunit gp16. Gp17 exhibits a weak ATPase activity, which is stimulated by 50-fold by gp16. Quantitative biochemical approaches were used to understand the mechanisms of ATPase. The T4 terminase with N-terminal gp17-ATPase catalytic center with its well-characterized functional motifs provided a good system to address the mechanism.

ISBN: 9780542655777Subjects--Topical Terms:

1017719
Biology, Molecular.

Biochemical mechanism of the DNA packaging ATPase from bacteriophage T4.
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100 1 $a Al-Zahrani, Abdulrahman S. $3 1295894
245 1 0 $a Biochemical mechanism of the DNA packaging ATPase from bacteriophage T4.
300 $a 113 p.
500 $a Adviser: Venigalla B. Rao.
500 $a Source: Dissertation Abstracts International, Volume: 67-04, Section: B, page: 1817.
502 $a Thesis (Ph.D.)--The Catholic University of America, 2006.
520 $a Terminases are enzymes common to many double-stranded DNA bacteriophages as well as eukaroytic DNA viruses. These enzymes excise a single viral genome from a concatemeric DNA precursor and package it into a preformed protective capsid by ATP hydrolysis. T4 terminase complex is comprised of the large subunit gp17 and the small subunit gp16. Gp17 exhibits a weak ATPase activity, which is stimulated by 50-fold by gp16. Quantitative biochemical approaches were used to understand the mechanisms of ATPase. The T4 terminase with N-terminal gp17-ATPase catalytic center with its well-characterized functional motifs provided a good system to address the mechanism.
520 $a The catalytic pathway for gp17-ATPase center was analyzed using specific mutants from our collection, which are predicted to be defective at defined steps of the catalytic pathway. A direct azido-ATP crosslinking approach was used to identify the number of ATP binding sites in gp16 and gp17. Walker-A mutants showed a loss of crosslinking with azido-ATP compound. Walker B mutants also showed a loss of crosslinking; but the mutants that retained the carboxylate group retained crosslinking. The Walker-B mutant data showed that merely binding ATP is not, as such, sufficient for catalysis; rather a precise orientation of ATP in the catalytic pocket is necessary to trigger catalysis. The N-360 domain showed azido-ATP crosslinking whereas the C-360 domain showed no crosslinking. The behavior of the mutant is consistent with the proposed roles of residues in the ATPase catalytic site. The binding site(s) of the small terminase, gp16 was investigated using a novel approach. ATP crosslinking to gp16 was influenced by the presence of gp17, indicating the specificity of ATP binding to gp16 and changes in the putative gp16-gp17 complex that influence gp16-ATP interaction. The terminases can also bind ADP and AMP with lower affinity than ATP.
520 $a Finally, a surprising finding was that the Walker-A mutants abolished the crosslinking of ATP to gp16, gp17, or gp17-mutants, which is not mediated by gp16. A model is postulated for the assembly of an oligomeric terminase complex, and dynamic interactions among the terminase subunits with the substrates and inhibitors to allosterically affect ATPase catalysis.
590 $a School code: 0043.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Engineering, Biomedical. $3 1017684
650 4 $a Health Sciences, Pharmacology. $3 1017717
690 $a 0307
690 $a 0419
690 $a 0487
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710 2 0 $a The Catholic University of America. $3 1019220
773 0 $t Dissertation Abstracts International $g 67-04B.
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791 $a Ph.D.
792 $a 2006
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