Lytic transglycosylases RlpA and MltC assist in Vibrio cholerae daughter cell separation.

Abstract:

:The cell wall is a crucial structural feature in the vast majority of bacteria and comprises a covalently closed network of peptidoglycan (PG) strands. While PG synthesis is important for survival under many conditions, the cell wall is also a dynamic structure, undergoing degradation and remodeling by 'autolysins', enzymes that break down PG. Cell division, for example, requires extensive PG remodeling, especially during separation of daughter cells, which depends heavily upon the activity of amidases. However, in Vibrio cholerae, we demonstrate that amidase activity alone is insufficient for daughter cell separation and that lytic transglycosylases RlpA and MltC both contribute to this process. MltC and RlpA both localize to the septum and are functionally redundant under normal laboratory conditions; however, only RlpA can support normal cell separation in low-salt media. The division-specific activity of lytic transglycosylases has implications for the local structure of septal PG, suggesting that there may be glycan bridges between daughter cells that cannot be resolved by amidases. We propose that lytic transglycosylases at the septum cleave PG strands that are crosslinked beyond the reach of the highly regulated activity of the amidase and clear PG debris that may block the completion of outer membrane invagination.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Weaver AI,Jiménez-Ruiz V,Tallavajhala SR,Ransegnola BP,Wong KQ,Dörr T

doi

10.1111/mmi.14349

subject

Has Abstract

pub_date

2019-10-01 00:00:00

pages

1100-1115

issue

4

eissn

0950-382X

issn

1365-2958

journal_volume

112

pub_type

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