Unknown

Dataset Information

0

Bacterial cell division regulation by Ser/Thr kinases: a structural perspective.


ABSTRACT: Recent genetic, biochemical and structural studies have established that eukaryotic-like Ser/Thr protein-kinases are critical mediators of developmental changes and host pathogen interactions in bacteria. Although with lower abundance compared to their homologues from eukaryotes, Ser/Thr protein-kinases are widespread in gram-positive bacteria. These data underline a key role of reversible Ser/Thr phosphorylation in bacterial physiology and virulence. Numerous studies have revealed how phosphorylation/dephosphorylation of Ser/Thr protein-kinases governs cell division and cell wall biosynthesis and that Ser/Thr protein kinases are responsible for distinct phenotypes, dependent on different environmental signals. In this review we discuss the current understandings of Ser/Thr protein-kinases functional processes based on structural data.

SUBMITTER: Ruggiero A 

PROVIDER: S-EPMC3601408 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Bacterial cell division regulation by Ser/Thr kinases: a structural perspective.

Ruggiero Alessia A   De Simone Paola P   Smaldone Giovanni G   Squeglia Flavia F   Berisio Rita R  

Current protein & peptide science 20121201 8


Recent genetic, biochemical and structural studies have established that eukaryotic-like Ser/Thr protein-kinases are critical mediators of developmental changes and host pathogen interactions in bacteria. Although with lower abundance compared to their homologues from eukaryotes, Ser/Thr protein-kinases are widespread in gram-positive bacteria. These data underline a key role of reversible Ser/Thr phosphorylation in bacterial physiology and virulence. Numerous studies have revealed how phosphory  ...[more]

Similar Datasets

| S-EPMC3326482 | biostudies-literature
| S-EPMC2154464 | biostudies-literature
| S-EPMC3705213 | biostudies-literature
| S-EPMC1262709 | biostudies-literature
| S-EPMC6506691 | biostudies-literature
| S-EPMC1223382 | biostudies-other
| S-EPMC6432918 | biostudies-literature