PMID- 10381378
OWN - NLM
STAT- MEDLINE
DCOM- 19990729
LR  - 20171116
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 260
IP  - 1
DP  - 1999 Jun 24
TI  - Characterization of five human cDNAs with homology to the yeast SIR2 gene:
      Sir2-like proteins (sirtuins) metabolize NAD and may have protein
      ADP-ribosyltransferase activity.
PG  - 273-9
AB  - The yeast Sir2 protein regulates epigenetic gene silencing and as a possible
      antiaging effect it suppresses recombination of rDNA. Studies involving cobB, a
      bacterial SIR2-like gene, have suggested it could encode a pyridine nucleotide
      transferase. Here five human sirtuin cDNAs are characterized. The SIRT1 sequence 
      has the closest homology to the S. cerevisiae Sir2p. The SIRT4 and SIRT5 sirtuins
      more closely resemble prokaryotic sirtuin sequences. The five human sirtuins are 
      widely expressed in fetal and adult tissues. Recombinant E. coli cobT and cobB
      proteins each showed a weak NAD-dependent mono-ADP-ribosyltransferase activity
      using 5, 6-dimethylbenzimidazole as a substrate. Recombinant E. coli cobB and
      human SIRT2 sirtuin proteins were able to cause radioactivity to be transferred
      from [32P]NAD to bovine serum albumin (BSA). When a conserved histidine within
      the human SIRT2 sirtuin was converted to a tyrosine, the mutant recombinant
      protein was unable to transfer radioactivity from [32P]NAD to BSA. These results 
      suggest that the sirtuins may function via mono-ADP-ribosylation of proteins.
CI  - Copyright 1999 Academic Press.
FAU - Frye, R A
AU  - Frye RA
AD  - Department of Pathology, University of Pittsburgh, Pittsburgh, Pennsylvania,
      15240, USA. frye01@pitt.edu
LA  - eng
SI  - GENBANK/AF083106
SI  - GENBANK/AF083107
SI  - GENBANK/AF083108
SI  - GENBANK/AF083109
SI  - GENBANK/AF083110
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (DNA, Complementary)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Multienzyme Complexes)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Silent Information Regulator Proteins, Saccharomyces cerevisiae)
RN  - 0 (Trans-Activators)
RN  - 27432CM55Q (Serum Albumin, Bovine)
RN  - EC 2.4.2.- (ADP Ribose Transferases)
RN  - EC 2.4.2.- (Pentosyltransferases)
RN  - EC 2.4.2.21 (nicotinate-nucleotide-dimethylbenzimidazole
      phosphoribosyltransferase)
RN  - EC 2.4.2.30 (Poly(ADP-ribose) Polymerases)
RN  - EC 2.7.7.- (Nucleotidyltransferases)
RN  - EC 3.5.1.- (SIR2 protein, S cerevisiae)
RN  - EC 3.5.1.- (SIRT1 protein, human)
RN  - EC 3.5.1.- (Sirtuin 1)
RN  - EC 3.5.1.- (Sirtuin 2)
RN  - EC 3.5.1.- (Sirtuins)
RN  - EC 3.5.1.98 (Histone Deacetylases)
SB  - IM
MH  - *ADP Ribose Transferases
MH  - Amino Acid Sequence
MH  - DNA, Complementary/*metabolism
MH  - DNA-Binding Proteins/*chemistry
MH  - *Histone Deacetylases
MH  - Humans
MH  - Molecular Sequence Data
MH  - *Multienzyme Complexes
MH  - *Nucleotidyltransferases
MH  - Pentosyltransferases/chemistry
MH  - Poly(ADP-ribose) Polymerases/*metabolism
MH  - Recombinant Proteins/metabolism
MH  - Saccharomyces cerevisiae/chemistry
MH  - Sequence Homology, Amino Acid
MH  - Serum Albumin, Bovine/metabolism
MH  - *Silent Information Regulator Proteins, Saccharomyces cerevisiae
MH  - Sirtuin 1
MH  - Sirtuin 2
MH  - Sirtuins
MH  - Tissue Distribution
MH  - Trans-Activators/*chemistry
EDAT- 1999/06/25 00:00
MHDA- 1999/06/25 00:01
CRDT- 1999/06/25 00:00
PHST- 1999/06/25 00:00 [pubmed]
PHST- 1999/06/25 00:01 [medline]
PHST- 1999/06/25 00:00 [entrez]
AID - 10.1006/bbrc.1999.0897 [doi]
AID - S0006-291X(99)90897-5 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Jun 24;260(1):273-9. doi:
      10.1006/bbrc.1999.0897.