2009
DOI: 10.1007/s12275-009-0032-y
|View full text |Cite
|
Sign up to set email alerts
|

Analysis and identification of ADP-ribosylated proteins of Streptomyces coelicolor M145

Abstract: Mono-ADP-ribosylation is the enzymatic transfer of ADP-ribose from NAD(+) to acceptor proteins catalyzed by ADP-ribosyltransferases. Using m-aminophenylboronate affinity chromatography, 2D-gel electrophoresis, in-gel digestion and MALDI-TOF analysis we have identified eight in vitro ADP-ribosylated proteins in Streptomyces coelicolor, which can be classified into three categories: (i) secreted proteins; (ii) metabolic enzymes using NAD(+)/NADH or NADP(+)/NADPH as coenzymes; and (iii) other proteins. The secret… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
9
0

Year Published

2012
2012
2022
2022

Publication Types

Select...
8

Relationship

0
8

Authors

Journals

citations
Cited by 11 publications
(9 citation statements)
references
References 37 publications
0
9
0
Order By: Relevance
“…5G), was not clearly biased toward MI or MII (Table S1). Some of these genes are well characterized, including glgP , a glycogen phosphorylase up-regulated in MII (up to 16-fold) which participates in glycogen and trehalose metabolism during sequential stages of aerial mycelium development [51] and SCO2008, encoding for a branched chain amino acid binding protein up-regulated in MII (up to 7-fold), which may participate in regulation of morphological differentiation in S. coelicolor [52]. Interestingly, most genes encoding for proteins of “unknown” function were up-regulated in MII (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…5G), was not clearly biased toward MI or MII (Table S1). Some of these genes are well characterized, including glgP , a glycogen phosphorylase up-regulated in MII (up to 16-fold) which participates in glycogen and trehalose metabolism during sequential stages of aerial mycelium development [51] and SCO2008, encoding for a branched chain amino acid binding protein up-regulated in MII (up to 7-fold), which may participate in regulation of morphological differentiation in S. coelicolor [52]. Interestingly, most genes encoding for proteins of “unknown” function were up-regulated in MII (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Here we confirmed auto mono-ADP-ribosylating activity of the SCO5461 protein in vitro , but its specific protein trans targets are yet to be discovered. Several identified ADP-ribosylated proteins in S. coelicolor suggested a connection between protein ADP-ribosylation and the regulation of metabolic requirements of the cells (25, 41). SCO5461 is not conserved across the Streptomyces species (including S. griseus ), suggesting that the major protein ADP-ribosyltransferases in Streptomyces are yet to be uncovered.…”
Section: Discussionmentioning
confidence: 99%
“…Being the best characterized, bacterial DraG (homologue of human ARH1 and ARH3) is a representative of the group of arginine-specific ADP-ribosylhydrolases whose homologues are distributed across all three domains of life. Endogenous ADP-ribosylation has also been reported for some other bacteria, Myxococcus xanthus (18, 19), Mycobacterium smegmatis (20), Bacillus subtilis (21), and Streptomyces representatives (2225), but little is known about its function in bacteria. Genomic evidence indicates that proteins involved in ADP-ribosylation processing are widespread among bacteria.…”
Section: Introductionmentioning
confidence: 99%
“…DraT homologues are restricted to several nitrogen‐fixing bacteria, while DraG homologues are distributed across all three domains of life . Endogenous ADP‐ribosylation has also been reported for some other bacterial species where this process probably regulates important cellular functions such as sporulation in Bacillus subtilis , development and cell–cell interaction in Myxococcus xanthus , as well as differentiation and secondary metabolism in Streptomyces .…”
Section: Adp‐ribosylation In Bacteriamentioning
confidence: 92%
“…griseus and Streptomyces coelicolor , ADP‐ribosylation patterns change with morphological differentiation and several identified ADP‐ribosylated proteins in Str. coelicolor suggested a connection between protein ADP‐ribosylation and the regulation of metabolic requirements of the cells .…”
Section: Adp‐ribosylation In Bacteriamentioning
confidence: 99%