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Novel regulators of the essential tu...

Handler, Aaron Asher.

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Novel regulators of the essential tubulin-like bacterial cell division protein FtsZ.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Novel regulators of the essential tubulin-like bacterial cell division protein FtsZ./
Author:	Handler, Aaron Asher.
Description:	282 p.
Notes:	Source: Dissertation Abstracts International, Volume: 67-05, Section: B, page: 2354.
Contained By:	Dissertation Abstracts International67-05B.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3217750
ISBN:	9780542692673

Novel regulators of the essential tubulin-like bacterial cell division protein FtsZ.
Handler, Aaron Asher.

Novel regulators of the essential tubulin-like bacterial cell division protein FtsZ. - 282 p.

Source: Dissertation Abstracts International, Volume: 67-05, Section: B, page: 2354.

Thesis (Ph.D.)--Harvard University, 2006.

Cytokinesis, or cell division, is a physiological process in which a living cell divides to form two identical or non-identical cell types. With few exceptions, cell division in bacteria is initiated by formation at the incipient division site of a circumferential ring of polymerized FtsZ known as the "Z-ring". The Z-ring serves as a scaffold for the recruitment of several essential cell division proteins and may provide the contractile force required for invagination of the cytoplasmic membrane, a step that culminates in the physical compartmentalization of the predivisional cell. FtsZ itself is widely conserved among both gram-negative and gram-positive bacteria and shares structural and functional similarity with eukaryotic tubulin.

ISBN: 9780542692673Subjects--Topical Terms:

1017719
Biology, Molecular.

Novel regulators of the essential tubulin-like bacterial cell division protein FtsZ.
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100 1 $a Handler, Aaron Asher. $3 1917906
245 1 0 $a Novel regulators of the essential tubulin-like bacterial cell division protein FtsZ.
300 $a 282 p.
500 $a Source: Dissertation Abstracts International, Volume: 67-05, Section: B, page: 2354.
500 $a Adviser: Richard Losick.
502 $a Thesis (Ph.D.)--Harvard University, 2006.
520 $a Cytokinesis, or cell division, is a physiological process in which a living cell divides to form two identical or non-identical cell types. With few exceptions, cell division in bacteria is initiated by formation at the incipient division site of a circumferential ring of polymerized FtsZ known as the "Z-ring". The Z-ring serves as a scaffold for the recruitment of several essential cell division proteins and may provide the contractile force required for invagination of the cytoplasmic membrane, a step that culminates in the physical compartmentalization of the predivisional cell. FtsZ itself is widely conserved among both gram-negative and gram-positive bacteria and shares structural and functional similarity with eukaryotic tubulin.
520 $a The gram positive bacterium Bacillus subtilis forms Z-rings either at the midcell position during vegetative growth, or at positions near each pole upon entry into sporulation, a specialized developmental process that leads to the formation of an environmentally resistant endospore. In both cases, a host of regulatory proteins ensure the correct spatiotemporal formation of the Z-ring by modulating FtsZ polymerization. The work described here is centered on two such cellular factors. The first of these factors is a recently discovered protein called ZapA that functions to promote Z-ring assembly by stabilizing FtsZ polymeric structures. I identified several amino acid residues essential for ZapA function and present evidence that these residues are involved in both ZapA dimer formation and FtsZ contact. Additionally, I present progress made toward the elucidation of the solution structure of the Bacillus stearothermophilus ZapA ortholog. The second factor is a peptide inhibitor of FtsZ polymerization called AahZ, which I discovered in a yeast two-hybrid screen design to uncover novel FtsZ-interacting proteins. I show that AahZ functions during sporulation in B. subtilis to prevent the formation of aberrant Z-rings, and shares similarity in sequence and function with an antimicrobial peptide produced in mouse called CRAMP. The convergence of AahZ and CRAMP, one a bacterial protein and the other a mammalian antimicrobial peptide, onto a common bacterial target, FtsZ, serves as a striking new example of conservation across widely separated species.
590 $a School code: 0084.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Microbiology. $3 1017734
690 $a 0307
690 $a 0410
710 2 0 $a Harvard University. $3 528741
773 0 $t Dissertation Abstracts International $g 67-05B.
790 1 0 $a Losick, Richard, $e advisor
790 $a 0084
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3217750