Abstract：
:Heart failure is the most common cause of morbidity and hospitalization in the western civilization. Protein phosphatases play a key role in the basal cardiac contractility and in the responses to β-adrenergic stimulation with type-1 phosphatase (PP-1) being major contributor. We propose here that formation of transient disulfide bridges in PP-1α might play a leading role in oxidative stress response. First, we established an optimized workflow, the so-called "cross-over-read" search method, for the identification of disulfide-linked species using permutated databases. By applying this method, we demonstrate the formation of unexpected transient disulfides in PP-1α to shelter against over-oxidation. This protection mechanism strongly depends on the fast response in the presence of reduced glutathione. Our work points out that the dimerization of PP-1α involving Cys39 and Cys127 is presumably important for the protection of PP-1α active surface in the absence of a substrate. We finally give insight into the electron transport from the PP-1α catalytic core to the surface. Our data suggest that the formation of transient disulfides might be a general mechanism of proteins to escape from irreversible cysteine oxidation and to prevent their complete inactivation.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Singh S,Lämmle S,Giese H,Kämmerer S,Meyer-Roxlau S,Alfar EA,Dihazi H,Guan K,El-Armouche A,Richter Fdoi
10.1038/s41598-018-36267-6subject
Has Abstractpub_date
2018-12-07 00:00:00pages
17711issue
1issn
2045-2322pii
10.1038/s41598-018-36267-6journal_volume
8pub_type
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