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Regulation of sporulation-specific transcription factors by proteolysis in Bacillus subtilis.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Regulation of sporulation-specific transcription factors by proteolysis in Bacillus subtilis.
作者:	Pan, Qi.
面頁冊數:	185 p.
附註:	Adviser: Richard Losick.
附註:	Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4338.
Contained By:	Dissertation Abstracts International64-09B.
標題:	Chemistry, Biochemistry.
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3106683
ISBN:	0496542486

Regulation of sporulation-specific transcription factors by proteolysis in Bacillus subtilis.
Pan, Qi.

Regulation of sporulation-specific transcription factors by proteolysis in Bacillus subtilis. [electronic resource] - 185 p.

Adviser: Richard Losick.

Thesis (Ph.D.)--Harvard University, 2003.

During my search for the SpoIIAB protease, I unexpectedly discovered a sporulation-specific carboxyl-terminal processing protease, CtpB, which is required for the efficient activation of sigmaK in the mother cell. Active sigmaK is derived by regulated proteolysis from the inactive proprotein, pro-sigmaK. Processing of pro-sigma K is triggered by an intercompartmental signal delivered by a forespore signaling protein SpoIVB. SpoIVB and CtpB are both serine proteases with PDZ domains, and are both predicted to be secreted into the intermembrane space between the mother cell and the forespore. CtpB is probably part of a fine-tuning mechanism that contributes to the timely and efficient processing of pro-sigma K.

ISBN: 0496542486Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

Regulation of sporulation-specific transcription factors by proteolysis in Bacillus subtilis.
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520 # $a During my search for the SpoIIAB protease, I unexpectedly discovered a sporulation-specific carboxyl-terminal processing protease, CtpB, which is required for the efficient activation of sigmaK in the mother cell. Active sigmaK is derived by regulated proteolysis from the inactive proprotein, pro-sigmaK. Processing of pro-sigma K is triggered by an intercompartmental signal delivered by a forespore signaling protein SpoIVB. SpoIVB and CtpB are both serine proteases with PDZ domains, and are both predicted to be secreted into the intermembrane space between the mother cell and the forespore. CtpB is probably part of a fine-tuning mechanism that contributes to the timely and efficient processing of pro-sigma K.
520 # $a How developmental transcription factors are activated is a fundamental question in biology. This thesis addresses the role of proteolysis on the regulation of alternative RNA polymerase sigma factors during sporulation in B. subtilis. A hallmark of sporulation is the formation of an asymmetrically localized septum that divides the sporulating cell into two unequal-sized compartments, the mother cell and the forespore. Four sporulation-specific sigma factors are activated in a spatially and temporally restricted fashion after polar septation to orchestrate gene expression during this developmental process. I focus my study on the function of proteolysis in the activation of sigmaF, the early-appearing forespore-specific sigma factor, and sigmaK, the late-appearing mother-cell-specific sigma factor.
520 # $a sigmaF is initially held in an inactive complex by the antisigma factor SpoIIAB. The anti-antisigma factor SpoIIAA reacts with the SpoIIAB·sigmaF complex in the forespore to induce the release of free active sigmaF and free SpoIIAB. The starting point for this thesis was the discovery that the sigma F activation pathway involves the proteolysis of SpoIIAB. Free SpoIIAB but not SpoIIAB when it is in a complex with sigmaF is subject to proteolysis. I was able to establish a correlation between the degree of SpoIIAB instability and sigmaF activity, which suggests that proteolysis of SpoIIAB plays an important role in the activation of sigma F. SpoIIAB proteolysis requires three residues located at the extreme C-terminus of the protein and is dependent on the ClpCP protease. The last three residues of SpoIIAB are both necessary and sufficient to direct ClpCP-dependent proteolysis. Although all evidence points to ClpCP as the SpoIIAB processing protease, I was not able to reconstitute ClpCP-mediated SpoIIAB degradation in vitro. These negative results suggest that ClpCP-mediated degradation of SpoIIAB may involve an unknown adaptor molecule.
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