دورية أكاديمية
أعرض في EDS

Cytological characterization of YpsB, a novel component of the Bacillus subtilis divisome.

التفاصيل البيبلوغرافية
العنوان: Cytological characterization of YpsB, a novel component of the Bacillus subtilis divisome.
المؤلفون: Tavares JR; Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, Av. Prof. Lineu Prestes 748, 05508-000 São Paulo, SP, Brazil., de Souza RF, Meira GL, Gueiros-Filho FJ
المصدر: Journal of bacteriology [J Bacteriol] 2008 Nov; Vol. 190 (21), pp. 7096-107. Date of Electronic Publication: 2008 Sep 05.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 2985120R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1098-5530 (Electronic) Linking ISSN: 00219193 NLM ISO Abbreviation: J Bacteriol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : American Society for Microbiology
مواضيع طبية MeSH: Bacillus subtilis/*metabolism , Bacterial Proteins/*metabolism , Cell Cycle Proteins/*metabolism, Amino Acid Sequence ; Bacillus subtilis/classification ; Bacillus subtilis/genetics ; Bacterial Proteins/genetics ; Cell Cycle Proteins/genetics ; Evolution, Molecular ; Molecular Sequence Data ; Mutation ; Phylogeny ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Amino Acid
مستخلص: Cell division in bacteria is carried out by an elaborate molecular machine composed of more than a dozen proteins and known as the divisome. Here we describe the characterization of a new divisome protein in Bacillus subtilis called YpsB. Sequence comparisons and phylogentic analysis demonstrated that YpsB is a paralog of the division site selection protein DivIVA. YpsB is present in several gram-positive bacteria and likely originated from the duplication of a DivIVA-like gene in the last common ancestor of bacteria of the orders Bacillales and Lactobacillales. We used green fluorescent protein microscopy to determine that YpsB localizes to the divisome. Similarly to that for DivIVA, the recruitment of YpsB to the divisome requires late division proteins and occurs significantly after Z-ring formation. In contrast to DivIVA, however, YpsB is not retained at the newly formed cell poles after septation. Deletion analysis suggests that the N terminus of YpsB is required to target the protein to the divisome. The high similarity between the N termini of YpsB and DivIVA suggests that the same region is involved in the targeting of DivIVA. YpsB is not essential for septum formation and does not appear to play a role in septum positioning. However, a ypsB deletion has a synthetic effect when combined with a mutation in the cell division gene ftsA. Thus, we conclude that YpsB is a novel B. subtilis cell division protein whose function has diverged from that of its paralog DivIVA.
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المشرفين على المادة: 0 (Bacterial Proteins)
0 (Cell Cycle Proteins)
0 (Recombinant Fusion Proteins)
تواريخ الأحداث: Date Created: 20080909 Date Completed: 20090119 Latest Revision: 20211020
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC2580690
DOI: 10.1128/JB.00064-08
PMID: 18776011
قاعدة البيانات: MEDLINE
الوصف
تدمد:1098-5530
DOI:10.1128/JB.00064-08