Proteins required for vacuolar function are targets of lysine polyphosphorylation in yeast.

Abstract:

:Polyphosphates (polyP) are long chains of inorganic phosphates that can be attached to lysine residues of target proteins as a nonenzymatic post-translational modification. This modification, termed polyphosphorylation, may be particularly prevalent in bacterial and fungal species that synthesize large quantities of polyP. In this study, we evaluated the polyphosphorylation status of over 200 candidate targets in Saccharomyces cerevisiae. We report eight new polyphosphorylated proteins that interact genetically and physically with previous targets implicated in ribosome biogenesis. The expanded target network includes vacuolar proteins Prb1 and Apl5, whose modification with polyP suggests a model for feedback regulation of polyP synthesis, while raising questions regarding the location of polyphosphorylation in vivo.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

McCarthy L,Bentley-DeSousa A,Denoncourt A,Tseng YC,Gabriel M,Downey M

doi

10.1002/1873-3468.13588

subject

Has Abstract

pub_date

2020-01-01 00:00:00

pages

21-30

issue

1

eissn

0014-5793

issn

1873-3468

journal_volume

594

pub_type

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