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Abstract
Protein phosphorylation is the best characterized post-translational modification that regulates almost all cellular processes through diverse mechanisms such as changing protein conformations, interactions, and localization. While the inventory for phosphorylation sites across different species has rapidly expanded, their functional role remains poorly investigated. Here, we combine 537,321 phosphosites from 40 eukaryotic species to identify highly conserved phosphorylation hotspot regions within domain families. Mapping these regions onto structural data reveals that they are often found at interfaces, near catalytic residues and tend to harbor functionally important phosphosites. Notably, functional studies of a phospho-deficient mutant in the C-terminal hotspot region within the ribosomal S11 domain in the yeast ribosomal protein uS11 shows impaired growth and defective cytoplasmic 20S pre-rRNA processing at 16 °C and 20 °C. Altogether, our study identifies phosphorylation hotspots for 162 protein domains suggestive of an ancient role for the control of diverse eukaryotic domain families.
Highlights
Protein phosphorylation is the best characterized post-translational modification that regulates almost all cellular processes through diverse mechanisms such as changing protein conformations, interactions, and localization
In order to study the conservation of protein phosphorylation within protein domain families, we collected protein phosphosite data from publicly available sources for a total of 40 eukaryotic species, including 11 animals, 19 fungi, 7 plants, and 3 apicomplexa species (Fig. 1a and Methods)
As most phosphosites tend to occur in disordered regions[12] it is not unexpected that the majority of sites are not found within protein domains
Summary
Protein phosphorylation is the best characterized post-translational modification that regulates almost all cellular processes through diverse mechanisms such as changing protein conformations, interactions, and localization. We combine 537,321 phosphosites from 40 eukaryotic species to identify highly conserved phosphorylation hotspot regions within domain families. Mapping these regions onto structural data reveals that they are often found at interfaces, near catalytic residues and tend to harbor functionally important phosphosites. Functional studies of a phosphodeficient mutant in the C-terminal hotspot region within the ribosomal S11 domain in the yeast ribosomal protein uS11 shows impaired growth and defective cytoplasmic 20S prerRNA processing at 16 °C and 20 °C. To perform a systematic analysis we compile here an expanded set of over 500,000 phosphosites across 40 eukaryotic species These phosphosites are mapped to protein domain regions allowing us to identify phosphorylation hotspots within 162 domain families. We show that the Rps14a-T119A mutant exhibits impaired growth at 16 and 20 °C, and is defective in cytoplasmic 20S pre-rRNA processing, uncovering a critical role for phosphorylation of this region during eukaryotic ribosome assembly
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