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Acetylome analysis of Bordetella pertussis reveals possible targets of novel BP0960 gene-encoded lysine deacetylase

ABSTRACT: Acetylation on ε-amino groups of lysine residues (N-ε-lysine acetylation) represents an important mechanism of post-translational regulation of protein function. However, its role and extent in the whooping cough agent Bordetella pertussis remain unknown. In this study, we analyzed the acetylomes of two bacterial mutants lacking putative lysine deacetylases encoded by genes BP0960 and BP3063 and compared them with the acetylome of wild-type B. pertussis. The results suggest that acetylation on lysine residues may modulate the activities of proteins involved in bacterial virulence and of multiple histone-like proteins.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Bordetella Pertussis (strain Tohama I / Atcc Baa-589 / Nctc 13251) Bacteria

DISEASE(S): Pertussis

SUBMITTER: Ivo Fabrik

LAB HEAD: Prof. Peter Sebo, PhD.

PROVIDER: PXD016384 | Pride | 2020-07-19

REPOSITORIES: Pride

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Bordetellapertussis Acetylome is Shaped by Lysine Deacetylase Bkd1.

Novak Jakub J Fabrik Ivo I Jurnecka David D Holubova Jana J Stanek Ondrej O Sebo Peter P

Journal of proteome research 20200731 9

Post-translational modifications of proteins enable swift physiological adaptation of cells to altered growth conditions and stress. Aside from protein phosphorylation, acetylation on ε-amino groups of lysine residues (N-ε-lysine acetylation) represents another important post-translational modification of proteins. For many bacterial pathogens, including the whooping cough agent Bordetella pertussis, the role and extent of protein acetylation remain to be defined. We expressed in < ...[more]

PMID: 32674575

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