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Biochem Biophys Res Commun. 2003 Sep 5;308(4):820-5.

Protein PknE, a novel transmembrane eukaryotic-like serine/threonine kinase from Mycobacterium tuberculosis.

Author information

1
Institut de Biologie et Chimie des Protéines, Université de Lyon, Centre National de la Recherche Scientifique, Lyon, France. virginie_molle@yahoo.fr

Abstract

Protein PknE from Mycobacterium tuberculosis has been overproduced and purified, and its biochemical properties have been analyzed. This protein is shown to be a eukaryotic-like (Hanks'-type) protein kinase with a structural organization similar to that of membrane-bound eukaryotic sensor serine/threonine kinases. It consists of a N-terminal catalytic domain located in the cytoplasm, linked via a single transmembrane-spanning region to an extracellular C-terminal domain. The full-length enzyme, as well as the cytosolic domain alone, can autophosphorylate on serine and threonine residues. Such autokinase activity requires the presence of a lysine residue at position 45 in subdomain II, which is known to be essential also for eukaryotic kinase activity. Involvement of PknE in the transduction of external signals into the cytosol of bacteria is proposed.

PMID:
12927792
DOI:
10.1016/s0006-291x(03)01476-1
[Indexed for MEDLINE]

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