Open AccessDivIVA uses an N‐terminal conserved region and two coiled‐coil domains to localize and sustain the polar growth in Corynebacterium glutamicum
Author(s) -
Letek Michal,
Fiuza María,
Ordóñez Efrén,
Villadangos Almudena F.,
Flärdh Klas,
Mateos Luís M.,
Gil José A.
Publication year - 2009
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2009.01679.x
Subject(s) - corynebacterium glutamicum , coiled coil , bacillus subtilis , linker , peptidoglycan , function (biology) , biology , mreb , domain (mathematical analysis) , protein domain , biophysics , microbiology and biotechnology , computational biology , biochemistry , cell , cell wall , genetics , bacteria , cytoskeleton , computer science , mathematics , mathematical analysis , gene , operating system
Corynebacterium glutamicum is a rod‐shaped actinomycete with a distinct model of peptidoglycan synthesis during cell elongation, which takes place at the cell poles and is sustained by the essential protein DivIVA CG ( C. glutamicum DivIVA). This protein contains a short conserved N‐terminal domain and two coiled‐coil regions: CC1 and CC2. Domain deletions and chimeric versions of DivIVA were used to functionally characterize the three domains, and all three were found to be essential for proper DivIVA CG function. However, in the presence of the N‐terminal domain from DivIVA CG , either of the two coiled‐coil domains of DivIVA CG could be replaced by the equivalent coiled‐coil domain of Bacillus subtilis DivIVA (DivIVA BS ) without affecting the function of the original DivIVA CG , and more than one domain had to be exchanged to lose function. Although no single domain was sufficient for subcellular localization or function, CC1 was mainly implicated in stimulating polar growth and CC2 in targeting to DivIVA CG assemblies at the cell poles in C. glutamicum .