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Mutation of the ATPase Domain in Bac...

Nguyen, Matthew.

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Mutation of the ATPase Domain in Bacteriophage Lambda Stabilizes the Enzyme for Structural and Functional Analysis of the DNA Packaging Motor.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Mutation of the ATPase Domain in Bacteriophage Lambda Stabilizes the Enzyme for Structural and Functional Analysis of the DNA Packaging Motor./
Author:	Nguyen, Matthew.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2020,
Description:	93 p.
Notes:	Source: Masters Abstracts International, Volume: 81-12.
Contained By:	Masters Abstracts International81-12.
Subject:	Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=27834723
ISBN:	9798645472306

Mutation of the ATPase Domain in Bacteriophage Lambda Stabilizes the Enzyme for Structural and Functional Analysis of the DNA Packaging Motor.
Nguyen, Matthew.

Mutation of the ATPase Domain in Bacteriophage Lambda Stabilizes the Enzyme for Structural and Functional Analysis of the DNA Packaging Motor. - Ann Arbor : ProQuest Dissertations & Theses, 2020 - 93 p.

Source: Masters Abstracts International, Volume: 81-12.

Thesis (M.S.)--California State University, Fullerton, 2020.

This item must not be sold to any third party vendors.

Terminase enzymes are responsible for packaging viral DNA into empty procapsids. Bacteriophage lambda (λ), a double-stranded DNA virus (dsDNA), utilizes a terminase holoenzyme that is composed of two subunits to package DNA. GpNu1, the smaller subunit, is responsible for site-specific assembly of viral DNA. GpA, the large subunit, is responsible for all the catalytic activity for the enzyme to begin viral assembly. To stabilize the gpA catalytic subunit, a dual point mutation was produced in the DNA packaging ATPase domain (D178E/E179D) and two truncations were made to remove 50 N terminal amino acids and 19 C terminal amino acids. The D178E/E179D mutations inactivate the ATPase domain and stabilize the protein for crystallography. The truncation at the N-terminus prevents interactions with the small subunit, while the truncation at the C-terminus prevents interactions with the viral capsid. Nuclease and helicase studies suggest that the N-terminal truncation destabilized the protein unless the D178E/E179D mutation was performed, which stabilized the mutant. DNA binding studies suggest that in the presence of viral DNA, the wild-type mutant binds to DNA much tighter than the D178E/E179D mutant. Preliminary crystallization structure solutions will confirm logical hypotheses formed about the gpA subunit and its interactions with DNA during viral assembly.

ISBN: 9798645472306Subjects--Topical Terms:

518028
Biochemistry.
Subjects--Index Terms:

Bacteriophage

Mutation of the ATPase Domain in Bacteriophage Lambda Stabilizes the Enzyme for Structural and Functional Analysis of the DNA Packaging Motor.
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245 1 0 $a Mutation of the ATPase Domain in Bacteriophage Lambda Stabilizes the Enzyme for Structural and Functional Analysis of the DNA Packaging Motor.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2020
300 $a 93 p.
500 $a Source: Masters Abstracts International, Volume: 81-12.
500 $a Advisor: Ortega, Marcos.
502 $a Thesis (M.S.)--California State University, Fullerton, 2020.
506 $a This item must not be sold to any third party vendors.
520 $a Terminase enzymes are responsible for packaging viral DNA into empty procapsids. Bacteriophage lambda (λ), a double-stranded DNA virus (dsDNA), utilizes a terminase holoenzyme that is composed of two subunits to package DNA. GpNu1, the smaller subunit, is responsible for site-specific assembly of viral DNA. GpA, the large subunit, is responsible for all the catalytic activity for the enzyme to begin viral assembly. To stabilize the gpA catalytic subunit, a dual point mutation was produced in the DNA packaging ATPase domain (D178E/E179D) and two truncations were made to remove 50 N terminal amino acids and 19 C terminal amino acids. The D178E/E179D mutations inactivate the ATPase domain and stabilize the protein for crystallography. The truncation at the N-terminus prevents interactions with the small subunit, while the truncation at the C-terminus prevents interactions with the viral capsid. Nuclease and helicase studies suggest that the N-terminal truncation destabilized the protein unless the D178E/E179D mutation was performed, which stabilized the mutant. DNA binding studies suggest that in the presence of viral DNA, the wild-type mutant binds to DNA much tighter than the D178E/E179D mutant. Preliminary crystallization structure solutions will confirm logical hypotheses formed about the gpA subunit and its interactions with DNA during viral assembly.
590 $a School code: 6060.
650 4 $a Biochemistry. $3 518028
650 4 $a Virology. $3 642304
653 $a Bacteriophage
653 $a DNA packaging
653 $a gpA
653 $a Lambda bacteriophage
653 $a Terminase
653 $a Virus
690 $a 0487
690 $a 0720
710 2 $a California State University, Fullerton. $b Chemistry. $3 3547608
773 0 $t Masters Abstracts International $g 81-12.
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791 $a M.S.
792 $a 2020
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=27834723