Structural basis for the inhibition of the chromatin repressor BAHD1 by the bacterial nucleomodulin LntA.

ABSTRACT:

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The nucleus has emerged as a key target for nucleomodulins, a family of effectors produced by bacterial pathogens to control host transcription or other nuclear processes. The virulence factor LntA from Listeria monocytogenes stimulates interferon responses during infection by inhibiting BAHD1, a nuclear protein involved in gene silencing by promoting heterochromatin formation. So far, whether the interaction between LntA and BAHD1 is direct and sufficient for inhibiting BAHD1 activity is unknown. Here, we functionally characterized the molecular interface between the two proteins in vitro and in transfected or infected human cells. Based on the known tridimensional structure of LntA, we identified a dilysine motif (K180/K181) in the elbow region of LntA and a central pr

SUBMITTER: Lebreton A 

PROVIDER: S-EPMC3903274 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature