Redox regulation of sirtuin-1 by S-glutathiolation.

Abstract:

:Sirtuin-1 (SIRT1) is an NAD(+)-dependent protein deacetylase that is sensitive to oxidative signals. Our purpose was to determine whether SIRT1 activity is sensitive to the low molecular weight nitrosothiol, S-nitrosoglutathione (GSNO), which can transduce oxidative signals into physiological responses. SIRT1 formed mixed disulfides with GSNO-Sepharose, and mass spectrometry identified several cysteines that are modified by GSNO, including Cys-67 which was S-glutathiolated. GSNO had no effect on basal SIRT1 deacetylase activity, but inhibited stimulation of activity by resveratrol (RSV) with an IC(50) of 69 microM. These observations indicate that S-glutathiolation of SIRT1 by low concentrations of reactive glutathione can modulate its enzymatic activity.

journal_name

Antioxid Redox Signal

authors

Zee RS,Yoo CB,Pimentel DR,Perlman DH,Burgoyne JR,Hou X,McComb ME,Costello CE,Cohen RA,Bachschmid MM

doi

10.1089/ars.2010.3251

subject

Has Abstract

pub_date

2010-10-01 00:00:00

pages

1023-32

issue

7

eissn

1523-0864

issn

1557-7716

journal_volume

13

pub_type

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