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Biophysical and structural character...

Ortega, Marcos Eduardo.

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Biophysical and structural characterization of bacteriophage lambda terminase: A DNA packaging enzyme.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Biophysical and structural characterization of bacteriophage lambda terminase: A DNA packaging enzyme./
Author:	Ortega, Marcos Eduardo.
Description:	126 p.
Notes:	Adviser: Carlos Enrique Catalano.
Contained By:	Dissertation Abstracts International67-08B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3230430
ISBN:	9780542847677

Biophysical and structural characterization of bacteriophage lambda terminase: A DNA packaging enzyme.
Ortega, Marcos Eduardo.

Biophysical and structural characterization of bacteriophage lambda terminase: A DNA packaging enzyme. - 126 p.

Adviser: Carlos Enrique Catalano.

Thesis (Ph.D.)--University of Colorado Health Sciences Center, 2006.

In sum, my studies have identified structural domains within the lambda terminase subunits and have shed light on the function of each protein in DNA packaging.

ISBN: 9780542847677Subjects--Topical Terms:

1019105
Biophysics, General.

Biophysical and structural characterization of bacteriophage lambda terminase: A DNA packaging enzyme.
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005 20110927
008 110927s2006 eng d
020 $a 9780542847677
035 $a (UnM)AAI3230430
035 $a AAI3230430
040 $a UnM $c UnM
100 1 $a Ortega, Marcos Eduardo. $3 1295947
245 1 0 $a Biophysical and structural characterization of bacteriophage lambda terminase: A DNA packaging enzyme.
300 $a 126 p.
500 $a Adviser: Carlos Enrique Catalano.
500 $a Source: Dissertation Abstracts International, Volume: 67-08, Section: B, page: 4411.
502 $a Thesis (Ph.D.)--University of Colorado Health Sciences Center, 2006.
520 $a In sum, my studies have identified structural domains within the lambda terminase subunits and have shed light on the function of each protein in DNA packaging.
520 $a The terminase enzyme from bacteriophage lambda is responsible for insertion of the viral genome into a capsid shell. Lambda terminase is composed of two subunits. The small subunit, gpNu1, is responsible for site-specific recognition of viral DNA, while the large subunit, gpA, possesses all the catalytic activities of the enzyme. My research has focused on a biophysical and structural characterization of the individual terminase subunits.
520 $a In the first part of this work, I demonstrate that residues 1--55 comprise the minimal DNA binding domain (DBD) of gpNu1, and that this construct forms a stable dimer under all conditions examined. The high-resolution solution structure of the gpNu1 DBD was solved in our lab, which identified a winged helix-turn-helix DNA-binding motif. Based on the structure of the gpNu1 DBD, our lab proposed a novel DNA-binding model that incorporates cooperative binding and bending of viral DNA by gpNu1 and the E. coli IHF protein to assemble the packaging motor.
520 $a In the second part of this work, I performed quantitative electrophoretic mobility shift (EMS) and circular permutation experiments to directly test the proposed DNA binding and bending model. While truncation proteins proved useful in defining structural domains in gpNu1, the DNA binding affinity and specificity of the constructs was greatly reduced. I therefore used the full-length protein to characterize gpNu1 DNA binding interactions. EMS studies showed that gpNu1 and IHF bound cos DNA cooperatively and that both proteins bend the duplex upon binding.
520 $a In the third part of this work, I focused on a biochemical and biophysical characterization of gpA. Limited-proteolysis studies identified five protease-resistant fragments of gpA and I have characterized a soluble C-terminal construct that encompasses the nuclease/helicase domain of the protein. I demonstrate that this domain binds DNA and possesses a weak nuclease activity that is stimulated by ATP. I further demonstrate that this construct contains a discrete ATPase catalytic site associated with the nuclease and helicase activities of the protein.
590 $a School code: 0831.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0487
690 $a 0786
710 2 0 $a University of Colorado Health Sciences Center. $3 1023815
773 0 $t Dissertation Abstracts International $g 67-08B.
790 $a 0831
790 1 0 $a Catalano, Carlos Enrique, $e advisor
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3230430