Both the transglycosylase and transpeptidase functions in plastid penicillin-binding protein are essential for plastid division in physcomitrella patens

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 (δpppbp) results in a macrochloroplast phenotype by affecting plastid division. here,expression of pppbp-gfp in apppbp 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.