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Production of CSF, an extracellular ...

Lanigan, Sara Lynn.

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Production of CSF, an extracellular signaling peptide of Bacillus subtilis.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Production of CSF, an extracellular signaling peptide of Bacillus subtilis./
Author:	Lanigan, Sara Lynn.
Description:	118 p.
Notes:	Adviser: Beth Lazazzera.
Contained By:	Dissertation Abstracts International68-01B.
Subject:	Biology, Microbiology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3249412

Production of CSF, an extracellular signaling peptide of Bacillus subtilis.
Lanigan, Sara Lynn.

Production of CSF, an extracellular signaling peptide of Bacillus subtilis. - 118 p.

Adviser: Beth Lazazzera.

Thesis (Ph.D.)--University of California, Los Angeles, 2006.

Bacillus subtilis, like other Gram-positive bacteria, use small, gene-encoded, secreted peptides to mediate quorum sensing. A quorum response is a change in gene expression made in a bacterial community due to sensing a high cell density. In B. subtilis the Phr family of peptides participate in quorum sensing by regulating processes that occur during the transition from exponential phase growth to stationary phase growth. These processes include sporulation, development of genetic competence, and biofilm formation. Phr peptides are produced as pre-pro-peptides that must be processed to release a mature Phr pentapeptide. The pre sequence, or signal sequence, is predicted to be cleaved by a signal peptidase during transport through the general secretion machinery. The subsequent removal of the pro domain has, until now, occurred by an unknown mechanism. Data presented in this study identifies three secreted, serine proteases, subtilisin, Epr, and Vpr, which are involved in production of mature Phr peptides. The data presented here also suggests that there is at least one other, as yet unidentified, serine protease involved in Phr production. The cleavage of one Phr peptide, CSF, by these serine proteases was shown in this study to be partially dependent on a five amino acid motif found in the pro domain of CSF. This amino acid motif appears to be responsible for protease recognition and cleavage. This study provides an increased understanding of how Phr peptides are produced in B. subtilis and possibly in other bacterial species as well.Subjects--Topical Terms:

1017734
Biology, Microbiology.

Production of CSF, an extracellular signaling peptide of Bacillus subtilis.
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005 20110523
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035 $a (UMI)AAI3249412
035 $a AAI3249412
040 $a UMI $c UMI
100 1 $a Lanigan, Sara Lynn. $3 1269297
245 1 0 $a Production of CSF, an extracellular signaling peptide of Bacillus subtilis.
300 $a 118 p.
500 $a Adviser: Beth Lazazzera.
500 $a Source: Dissertation Abstracts International, Volume: 68-01, Section: B, page: 0075.
502 $a Thesis (Ph.D.)--University of California, Los Angeles, 2006.
520 $a Bacillus subtilis, like other Gram-positive bacteria, use small, gene-encoded, secreted peptides to mediate quorum sensing. A quorum response is a change in gene expression made in a bacterial community due to sensing a high cell density. In B. subtilis the Phr family of peptides participate in quorum sensing by regulating processes that occur during the transition from exponential phase growth to stationary phase growth. These processes include sporulation, development of genetic competence, and biofilm formation. Phr peptides are produced as pre-pro-peptides that must be processed to release a mature Phr pentapeptide. The pre sequence, or signal sequence, is predicted to be cleaved by a signal peptidase during transport through the general secretion machinery. The subsequent removal of the pro domain has, until now, occurred by an unknown mechanism. Data presented in this study identifies three secreted, serine proteases, subtilisin, Epr, and Vpr, which are involved in production of mature Phr peptides. The data presented here also suggests that there is at least one other, as yet unidentified, serine protease involved in Phr production. The cleavage of one Phr peptide, CSF, by these serine proteases was shown in this study to be partially dependent on a five amino acid motif found in the pro domain of CSF. This amino acid motif appears to be responsible for protease recognition and cleavage. This study provides an increased understanding of how Phr peptides are produced in B. subtilis and possibly in other bacterial species as well.
590 $a School code: 0031.
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Biology, Molecular. $3 1017719
690 $a 0307
690 $a 0410
710 2 $a University of California, Los Angeles. $3 626622
773 0 $t Dissertation Abstracts International $g 68-01B.
790 $a 0031
790 1 0 $a Lazazzera, Beth, $e advisor
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3249412