期刊
PROCEEDINGS OF THE JAPAN ACADEMY SERIES B-PHYSICAL AND BIOLOGICAL SCIENCES
卷 92, 期 10, 页码 499-508出版社
JAPAN ACAD
DOI: 10.2183/pjab.92.499
关键词
chloroplast division; penicillin-binding protein; Physcomitrella patens; transglycosylase; transpeptidase
资金
- Japan Society for the Promotion of Science KAKENHI [25440158, 26117720, 15K07130]
- Grants-in-Aid for Scientific Research [26117720, 25440158, 15K07130] Funding Source: KAKEN
Class A penicillin-binding proteins (PBPs) are active in the final step of bacterial peptidoglycan biosynthesis. They possess a transglycosylase (TG) domain to polymerize the glycan chains and a transpeptidase (TP) domain to catalyze peptide cross-linking. We reported that knockout of the Pbp gene in the moss Physcomitrella patens (Delta PpPbp) results in a macrochloroplast phenotype by affecting plastid division. Here, expression of PpPBP-GFP in Delta PpPbp restored the wild-type phenotype and GFP fluorescence was observed mainly in the periphery of each chloroplast. Stable transformants expressing Anabaena PBP with the plastid-targeting sequence, or PpPBP replacing the Anabaena TP domain exhibited partial recovery, while chloroplast number was recovered to that of wild-type plants in the transformant expressing PpPBP replacing the Anabaena TG domain. Transient expression experiments with site-directed mutagenized PpPBP showed that mutations in the conserved amino acids in both domains interfered with phenotype recovery. These results suggest that both TG and TP functions are essential for function of PpPBP in moss chloroplast division.
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