東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Functional studies of acyl carrier p...

Delay, Nicholas R.

Linked to FindBook

Google Book

Amazon

博客來

Functional studies of acyl carrier protein and the phosphopantetheinyl transferase AcpT in Escherichia coli K-12.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Functional studies of acyl carrier protein and the phosphopantetheinyl transferase AcpT in Escherichia coli K-12./
Author:	Delay, Nicholas R.
Description:	134 p.
Notes:	Adviser: John E. Cronan, Jr.
Contained By:	Dissertation Abstracts International68-07B.
Subject:	Biology, Microbiology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3269877
ISBN:	9780549095231

Functional studies of acyl carrier protein and the phosphopantetheinyl transferase AcpT in Escherichia coli K-12.
Delay, Nicholas R.

Functional studies of acyl carrier protein and the phosphopantetheinyl transferase AcpT in Escherichia coli K-12. - 134 p.

Adviser: John E. Cronan, Jr.

Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2007.

Acyl carrier protein (ACP) is a small, acidic protein that shuttles intermediates between fatty acid biosynthetic enzymes. Escherichia coli ACP is post-translationally modified by the enzyme AcpS which transfers a 4'-phosphopantetheine group from CoA to a conserved serine residue on the carrier protein. The thiol group provided by the phosphopantetheinyl moiety is the attachment site for biosynthetic intermediates being shuttled by the carrier protein between fatty acid biosynthetic enzymes.

ISBN: 9780549095231Subjects--Topical Terms:

1017734
Biology, Microbiology.

Functional studies of acyl carrier protein and the phosphopantetheinyl transferase AcpT in Escherichia coli K-12.
LDR:03225nam 2200301 a 45 001 969708
005 20110920
008 110921s2007 eng d
020 $a 9780549095231
035 $a (UMI)AAI3269877
035 $a AAI3269877
040 $a UMI $c UMI
100 1 $a Delay, Nicholas R. $3 1293765
245 1 0 $a Functional studies of acyl carrier protein and the phosphopantetheinyl transferase AcpT in Escherichia coli K-12.
300 $a 134 p.
500 $a Adviser: John E. Cronan, Jr.
500 $a Source: Dissertation Abstracts International, Volume: 68-07, Section: B, page: .
502 $a Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2007.
520 $a Acyl carrier protein (ACP) is a small, acidic protein that shuttles intermediates between fatty acid biosynthetic enzymes. Escherichia coli ACP is post-translationally modified by the enzyme AcpS which transfers a 4'-phosphopantetheine group from CoA to a conserved serine residue on the carrier protein. The thiol group provided by the phosphopantetheinyl moiety is the attachment site for biosynthetic intermediates being shuttled by the carrier protein between fatty acid biosynthetic enzymes.
520 $a The lack of a conditional mutant of acpP, the gene encoding E. coli ACP, was an obstacle preventing thorough in vivo studies of the functions of ACP and the importance of particular residues of ACP in performing these functions. I have isolated and characterized three temperature-sensitive acpP mutants of E. coli. I have tested several site directed mutants of E. coli ACP and ACPs from several diverse bacterial and eukaryotic species for the ability to complement one of these acpP(Ts) mutants. I found that several mutant ACPs containing substitutions of ACP residues previously reported to be required for ACP function in vitro support normal growth of the acpP mutant. All of the bacterial ACPs tested restored growth to the E. coli acpP mutant strain except those from, Enterococcus faecalis and Lactococcus lactis. Only one of the three eukaryotic organellar ACPs allowed growth.
520 $a A phosphopantetheinyl transferase called AcpT, which is encoded in the genome of E. coli strains, was previously reported to suppress an acpS mutant upon overexpression, but the purified AcpT failed to modify E. coli ACP in vitro. I have found that the growth of E. coli in the absence of AcpS activity is dependent on having a functional copy of acpT. I have also identified two carrier protein substrates for AcpT that are encoded in the genome of E. coli O157:H7.
520 $a Overexpression of AcpT was reported to suppress an E. coli K-12 mutant that has a temperature-sensitive phenotype and lipid A biosynthetic defect. I have mapped the mutation responsible for the lipid A biosynthetic defect and temperature-sensitive phenotype of this strain and have further characterized the suppression of the temperature-sensitive phenotype of strain LH530 by overexpression of AcpT.
590 $a School code: 0090.
650 4 $a Biology, Microbiology. $3 1017734
690 $a 0410
710 2 0 $a University of Illinois at Urbana-Champaign. $3 626646
773 0 $t Dissertation Abstracts International $g 68-07B.
790 $a 0090
790 1 0 $a Cronan, John E., Jr., $e advisor
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3269877