دورية أكاديمية
أعرض في EDS

Expression of Cds4/5 of Arabidopsis chloroplasts in E. coli reveals the membrane topology of the C-terminal region of CDP-diacylglycerol synthases.

التفاصيل البيبلوغرافية
العنوان: Expression of Cds4/5 of Arabidopsis chloroplasts in E. coli reveals the membrane topology of the C-terminal region of CDP-diacylglycerol synthases.
المؤلفون: Sekiya Y; Department of Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University, Morioka, Japan., Sawasato K; Department of Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University, Morioka, Japan., Nishiyama KI; Department of Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University, Morioka, Japan.
المصدر: Genes to cells : devoted to molecular & cellular mechanisms [Genes Cells] 2021 Sep; Vol. 26 (9), pp. 727-738. Date of Electronic Publication: 2021 Jul 06.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Blackwell Science Ltd Country of Publication: England NLM ID: 9607379 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1365-2443 (Electronic) Linking ISSN: 13569597 NLM ISO Abbreviation: Genes Cells Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Oxford, UK : Blackwell Science Ltd., 1996-
مواضيع طبية MeSH: Arabidopsis Proteins/*chemistry , Chloroplasts/*genetics , Diacylglycerol Cholinephosphotransferase/*chemistry, Arabidopsis ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Chloroplasts/metabolism ; Diacylglycerol Cholinephosphotransferase/genetics ; Diacylglycerol Cholinephosphotransferase/metabolism ; Escherichia coli ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Genetic Complementation Test ; Protein Domains
مستخلص: CDP-diacylglycerol synthases (Cds) are conserved from bacteria to eukaryotes. Bacterial CdsA is involved not only in phospholipid biosynthesis but also in biosynthesis of glycolipid MPIase, an essential glycolipid that catalyzes membrane protein integration. We found that both Cds4 and Cds5 of Arabidopsis chloroplasts complement cdsA knockout by supporting both phospholipid and MPIase biosyntheses. Comparison of the sequences of CdsA and Cds4/5 suggests a difference in membrane topology at the C-termini, since the region assigned as the last transmembrane region of CdsA, which follows the conserved cytoplasmic domain, is missing in Cds4/5. Deletion of the C-terminal region abolished the function, indicating the importance of the region. Both 6 × His tag attachment to CdsA and substitution of the C-terminal 6 residues with 6 × His did not affect the function. These 6 × His tags were sensitive to protease added from the cytosolic side in vitro, indicating that this region is not a transmembrane one but forms a membrane-embedded reentrant loop. Thus, the C-terminal region of Cds homologues forms a reentrant loop, of which structure is important for the Cds function.
(© 2021 Molecular Biology Society of Japan and John Wiley & Sons Australia, Ltd.)
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معلومات مُعتمدة: 15KT0073 Japan Society for the Promotion of Science; 16H01374 Japan Society for the Promotion of Science; 16K15083 Japan Society for the Promotion of Science; 17H02209 Japan Society for the Promotion of Science; 18KK0197 Japan Society for the Promotion of Science
فهرسة مساهمة: Keywords: Arabidopsis thaliana; E. coli; CDP-DAG synthase; Cds4/5; CdsA; MPIase; chloroplasts; membrane protein integration; phospholipid biosynthesis; transmembrane stretch
المشرفين على المادة: 0 (Arabidopsis Proteins)
0 (Escherichia coli Proteins)
EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase)
تواريخ الأحداث: Date Created: 20210624 Date Completed: 20211228 Latest Revision: 20211228
رمز التحديث: 20231215
DOI: 10.1111/gtc.12880
PMID: 34166546
قاعدة البيانات: MEDLINE
الوصف
تدمد:1365-2443
DOI:10.1111/gtc.12880