Phosphoproteomics of Streptococcsus suis serotype 2 wild-type strain ZY05719 and stk-deficient strain by label-free mass spectrometry
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ABSTRACT: To identify potential substrates of STK and their target phosphorylation sites in SS2, phosphoproteomic analysis was performed. A comparison of phosphorylated peptides from the WT strain (ZY05719) to those in the mutant strain (Δstk) helped us to identify phosphopeptides that disappeared or decreased in the mutant strain Δstk and are likely substrates of STK. In total, 41 unique phosphopeptides from 31 proteins were identified in S. suis lysates. Among the identified phosphopeptides, 44 phosphorylation sites were identified: 16 on serine, 23 on threonine and 5 on tyrosine. The phosphopeptides were considered to be phosphorylated by STK. Eleven phosphopeptides corresponding to 9 proteins had decreased phosphorylation in the Δstk strain. Twenty phosphopeptides corresponding to 14 proteins were only identified in the wild-type strain ZY05719. Because of the level of phosphorylation changes, these proteins may be STK target proteins that are phosphorylated in vivo.
ORGANISM(S): Streptococcus Suis
SUBMITTER: Hongjie Fan
PROVIDER: PXD022306 | iProX | Tue Nov 03 00:00:00 GMT 2020
REPOSITORIES: iProX
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