期刊
NEW PHYTOLOGIST
卷 -, 期 -, 页码 -出版社
WILEY
DOI: 10.1111/nph.19268
关键词
chloroplast division; penicillin-binding protein (PBP); peptidoglycan biosynthesis; Physcomitrium patens; PLASTID DIVISION2 (PDV2)
This study provides molecular evidence for the link between chloroplast division and PG biosynthesis in P. patens, suggesting that PG biosynthesis is required for the constriction of the chloroplast division apparatus.
center dot The peptidoglycan (PG) layer, a core component of the bacterial cell wall, has been retained in the Physcomitrium patens chloroplasts. The PG layer entirely encompasses the P. patens chloroplast, including the division site, but how PG biosynthesis cooperates with the constriction of two envelope membranes at the chloroplast division site remains elusive. center dot Here, focusing on the PG synthase penicillin-binding protein (PBP), we performed cytological and molecular analyses to dissect the mechanism of chloroplast division in P. patens. center dot We showed that PBP, acting in the final step of PG biosynthesis, is likely a chloroplast inner envelope protein that can aggregate at mid-chloroplasts during chloroplast division. Physcomitrium patens had five orthologs of PLASTID DIVISION2 (PDV2), an outer envelope component of the chloroplast division complex. Our data indicated that PpPDV2 proteins interact with PpPBP and are responsible for recruiting PpPBP to the chloroplast division site, in addition to PpDRP5B. Furthermore, we found that PBP deletion and carbenicillin application restrain constriction of the chloroplast division complex, rather than its assembly. center dot This work provides direct molecular evidence for a link between chloroplast division of P. patens and PG biosynthesis and indicates that PG biosynthesis is required for the constriction of the chloroplast division apparatus in P. patens.
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