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Proteins required for vacuolar function are targets of lysine polyphosphorylation in yeast
Author(s) -
McCarthy Liam,
BentleyDeSousa Amanda,
Decourt Alix,
Tseng YiChieh,
Gabriel Matthew,
Downey Michael
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13588
Subject(s) - lysine , biogenesis , yeast , saccharomyces cerevisiae , ribosome biogenesis , biochemistry , ribosome , function (biology) , chemistry , translation (biology) , posttranslational modification , biology , microbiology and biotechnology , gene , amino acid , rna , enzyme , messenger rna
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 .