SOBER1 explained

Symbol:SOBER1
Scop:6avv
Cath:6avv
Interpro:IPR029058

SOBER1 is an enzyme that catalyzes the biochemical reaction of deacetylation.[1] The SOBER (Suppressor of AvrBsT-elicited resistance) 1 protein is conserved in plants and it suppresses the plant's ability to carry out the hypersensitive response against infection by certain pathogenic effector proteins from the YopJ family.[2] SOBER1 belongs to the protein superfamily of α/β hydrolases and possesses a canonical serine/histidine/aspartate catalytic triad to carry out the deacetylation reaction. There have been contradicting reports about SOBER1's potential phospholipase activity, with one study claiming phospholipase A2 activity of the protein[3] and another study being unable to reproduce this result.

Relationship to acyl-protein thioesterases

Members of the SOBER1 family are considered closely related to acyl-protein thioesterases, judged by their protein structure. However, a change in their amino acid sequence renders SOBER1's biochemical properties into a deacetylase; in particular the hydrophobic tunnel, which is found in acyl-protein thioesterases, is impaired by additional amino acids in the lid structure of SOBER1, creating a new surface for binding of the acetyl group.

Targets

So far, the following proteins have been identified as SOBER1 targets: AvrBsT; ACIP1.

See also

Notes and References

  1. Bürger M, Willige BC, Chory J . A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors . Nature Communications . 8 . 1 . 2201 . December 2017 . 29259199 . 5736716 . 10.1038/s41467-017-02347-w . 2017NatCo...8.2201B .
  2. Cunnac S, Wilson A, Nuwer J, Kirik A, Baranage G, Mudgett MB . A conserved carboxylesterase is a SUPPRESSOR OF AVRBST-ELICITED RESISTANCE in Arabidopsis . The Plant Cell . 19 . 2 . 688–705 . February 2007 . 17293566 . 1867326 . 10.1105/tpc.106.048710 .
  3. Kirik A, Mudgett MB . SOBER1 phospholipase activity suppresses phosphatidic acid accumulation and plant immunity in response to bacterial effector AvrBsT . Proceedings of the National Academy of Sciences of the United States of America . 106 . 48 . 20532–7 . December 2009 . 19918071 . 2787154 . 10.1073/pnas.0903859106 . 2009PNAS..10620532K . free .