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The Function of TerC Proteins in Metal Homeostasis.
Sommaire Infos
The Function of TerC Proteins in Metal Homeostasis.
자료유형  
 학위논문
Control Number  
0017161166
International Standard Book Number  
9798382841731
Dewey Decimal Classification Number  
576
Main Entry-Personal Name  
He, Bixi.
Publication, Distribution, etc. (Imprint  
[S.l.] : Cornell University., 2024
Publication, Distribution, etc. (Imprint  
Ann Arbor : ProQuest Dissertations & Theses, 2024
Physical Description  
195 p.
General Note  
Source: Dissertations Abstracts International, Volume: 85-12, Section: B.
General Note  
Advisor: Helmann, John.
Dissertation Note  
Thesis (Ph.D.)--Cornell University, 2024.
Summary, Etc.  
요약Bacillus subtilis is a Gram-positive model organism found worldwide in environments with different nutrients and trace elements. To adapt to these changing growth conditions, B. subtilis has a high capacity for protein secretion and employs various systems to maintain the intracellular metal levels. Manganese is an important transition metal and functions as the cofactor in different metalloenzymes. Cytosolic Mn-requiring enzymes can acquire metals from buffered intracellular pools, but the mechanisms of metalation of exported enzymes are unclear. Here, we show that widely conserved TerC family proteins function in metalation of exoenzymes during or after their secretion process through the general secretion (Sec-dependent) pathway. B. subtilis cells lacking MeeF and MeeY have a reduced capacity for protein secretion and a dramatically reduced level of manganese in the secreted proteome. In the absence of TerC proteins, misfolded or unfolded proteins may stall the secretion translocon (SecYEG). The membrane protease FtsH, which can degrade dysfunctional SecY, is essential for cell viability. MeeF and MeeY can also influence the efficient function of Mn-dependent lipoteichoic acid synthase LtaS by metalation of Mn into its extracytoplasmic active site. Overall, MeeF and MeeY have functions in the co-translocational metalation of Mn-requiring membrane and extracellular enzymes (Chapter 2). The jamming of translocon caused by a lack of TerC proteins MeeF and MeeY may influence other cellular processes in B. subtilis. We provide evidence that MeeF and MeeY are involved in the swarming, sporulation, and natural competence. The double mutant meeFmeeY has defective swarming motility and decreased flagella production. Besides, cells lacking MeeF and MeeY in CU1065 strain background show defects in sporulation and a lower transformation efficiency. These defects indicate that clients other than LtaS require TerC proteins for metalation, and the impaired secretion in the cells without TerC proteins can cause pleiotropic phenotypes in B. subtilis (Chapter 3). Finally, we discuss the strategies employed by bacterial cells to metalate membrane-bound and secreted metalloenzymes which are involved in cell envelope homeostasis (Chapter 4).
Subject Added Entry-Topical Term  
Microbiology.
Subject Added Entry-Topical Term  
Cellular biology.
Subject Added Entry-Topical Term  
Molecular biology.
Index Term-Uncontrolled  
Bacillus subtilis
Index Term-Uncontrolled  
Protein secretion
Index Term-Uncontrolled  
Metalloenzymes
Index Term-Uncontrolled  
Extracellular enzymes
Added Entry-Corporate Name  
Cornell University Microbiology
Host Item Entry  
Dissertations Abstracts International. 85-12B.
Electronic Location and Access  
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Control Number  
joongbu:654266
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