CdsA, a CDP-diacylglycerol synthase involved in phospholipid and glycolipid MPIase biosynthesis, possesses multiple initiation codons.

التفاصيل البيبلوغرافية
العنوان:	CdsA, a CDP-diacylglycerol synthase involved in phospholipid and glycolipid MPIase biosynthesis, possesses multiple initiation codons.
المؤلفون:	Hikage R; Department of Applied Biological Chemistry, Faculty of Agriculture, Iwate University, Morioka, Japan., Sekiya Y; Department of Applied Biological Chemistry, Faculty of Agriculture, Iwate University, Morioka, Japan., Sawasato K; Department of Applied Biological Chemistry, Faculty of Agriculture, Iwate University, Morioka, Japan., Nishiyama KI; Department of Applied Biological Chemistry, Faculty of Agriculture, Iwate University, Morioka, Japan.
المصدر:	Genes to cells : devoted to molecular & cellular mechanisms [Genes Cells] 2024 Apr; Vol. 29 (4), pp. 347-355. Date of Electronic Publication: 2024 Feb 13.
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:	Diacylglycerol Cholinephosphotransferase/metabolism , Phospholipids , Glycolipids*, Codon, Initiator/genetics ; Codon, Terminator/genetics ; Protein Biosynthesis
مستخلص:	CdsA is a CDP-diacylglycerol synthase essential for phospholipid and glycolipid MPIase biosynthesis, and therefore for growth. The initiation codon of CdsA has been assigned as "TTG," while methionine at the 37th codon was reported to be an initiation codon in the original report. Since a vector containing the open reading frame starting with "TTG" under a controllable promoter complemented the cdsA knockout, "TTG" could function as an initiation codon. However, no evidence supporting that this "TTG" is the sole initiation codon has been reported. We determined the initiation codon by examining the ability of mutants around the N-terminal region to complement cdsA mutants. Even if the "TTG" was substituted with a stop codon, the clear complementation was observed. Moreover, the clones with multiple mutations of stop codons complemented the cdsA mutant up to the 37th codon, indicating that cdsA possesses multiple codons that can function as initiation codons. We constructed an experimental system in which the chromosomal expression of cdsA can be analyzed. By means of this system, we found that the cdsA mutant with substitution of "TTG" with a stop codon is fully functional. Thus, we concluded that CdsA contains multiple initiation codons. (© 2024 The Authors. Genes to Cells published by Molecular Biology Society of Japan and John Wiley & Sons Australia, Ltd.)
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معلومات مُعتمدة:	22H02567 Japan Society for the Promotion of Science; 22H05392 Japan Society for the Promotion of Science; 22K19262 Japan Society for the Promotion of Science; 23H04536 Japan Society for the Promotion of Science
فهرسة مساهمة:	Keywords: CDP‐diacylglycerol synthase; CdsA; MPIase; initiation codon; phospholipids
المشرفين على المادة:	EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase) 0 (Phospholipids) 0 (glycolipid MPIase) 0 (Codon, Initiator) 0 (Codon, Terminator) 0 (Glycolipids)
تواريخ الأحداث:	Date Created: 20240214 Date Completed: 20240404 Latest Revision: 20240404
رمز التحديث:	20240404
DOI:	10.1111/gtc.13104
PMID:	38351722
قاعدة البيانات:	MEDLINE

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تدمد:	1365-2443
DOI:	10.1111/gtc.13104