Topological characterization of the essential Escherichia coli cell division protein FtsN - PubMed (original) (raw)

Topological characterization of the essential Escherichia coli cell division protein FtsN

K Dai et al. J Bacteriol. 1996 Mar.

Abstract

Genetic and biochemical approaches were used to analyze a topological model for FtsN, a 36-kDa protein with a putative transmembrane segment near the N terminus, and to ascertain the requirements of the putative cytoplasmic and membrane-spanning domains for the function of this protein. Analysis of FtsN-PhoA fusions revealed that the putative transmembrane segment of FtsN could act as a translocation signal. Protease accessibility studies of FtsN in spheroblasts and inverted membrane vesicles confirmed that FtsN had a simple bitopic topology with a short cytoplasmic amino terminus, a single membrane-spanning domain, and a large periplasmic carboxy terminus. To ascertain the functional requirements of the N-terminal segments of FtsN, various constructs were made. Deletion of the N-terminal cytoplasmic and membrane-spanning domains led to intracellular localization of the carboxy domain, instability,and loss of function. Replacement of the N-terminal cytoplasmic and membrane-spanning domains with a membrane-spanning domain from MalG restored subcellular localization and function. These N-terminal domains of FtsN could also be replaced by the cleavable MalE signal sequence with restoration of subcellular localization and function. It is concluded that the N-terminal, cytoplasmic, and transmembrane domains of FtsN are not required for function of the carboxy domain other than to transport it to the periplasm. FtsQ and FtsI were also analyzed.

PubMed Disclaimer

Cited by

FtsN maintains active septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthases in E. coli.
Lyu Z, Yahashiri A, Yang X, McCausland JW, Kaus GM, McQuillen R, Weiss DS, Xiao J. Lyu Z, et al. Nat Commun. 2022 Sep 30;13(1):5751. doi: 10.1038/s41467-022-33404-8. Nat Commun. 2022. PMID: 36180460 Free PMC article.
Z-ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay.
Corbin BD, Geissler B, Sadasivam M, Margolin W. Corbin BD, et al. J Bacteriol. 2004 Nov;186(22):7736-44. doi: 10.1128/JB.186.22.7736-7744.2004. J Bacteriol. 2004. PMID: 15516588 Free PMC article.
Septal localization of FtsQ, an essential cell division protein in Escherichia coli.
Chen JC, Weiss DS, Ghigo JM, Beckwith J. Chen JC, et al. J Bacteriol. 1999 Jan;181(2):521-30. doi: 10.1128/JB.181.2.521-530.1999. J Bacteriol. 1999. PMID: 9882666 Free PMC article.
Membrane-bound division proteins DivIB and DivIC of Bacillus subtilis function solely through their external domains in both vegetative and sporulation division.
Katis VL, Wake RG. Katis VL, et al. J Bacteriol. 1999 May;181(9):2710-8. doi: 10.1128/JB.181.9.2710-2718.1999. J Bacteriol. 1999. PMID: 10217758 Free PMC article.

References

1. Nature. 1992 Sep 17;359(6392):251-4 - PubMed
1. Nature. 1991 Nov 14;354(6349):161-4 - PubMed
1. J Bacteriol. 1992 Oct;174(19):6145-51 - PubMed
1. J Bacteriol. 1992 Oct;174(19):6314-6 - PubMed
1. J Bacteriol. 1992 Dec;174(23):7716-28 - PubMed

Topological characterization of the essential Escherichia coli cell division protein FtsN - PubMed (original) (raw)