PMID- 25037163
OWN - NLM
STAT- MEDLINE
DCOM- 20150603
LR  - 20200826
IS  - 1465-2080 (Electronic)
IS  - 1350-0872 (Linking)
VI  - 160
IP  - Pt 10
DP  - 2014 Oct
TI  - Characterization of a dual-active enzyme, DcpA, involved in cyclic diguanosine 
      monophosphate turnover in Mycobacterium smegmatis.
PG  - 2304-2318
LID - 10.1099/mic.0.080200-0 [doi]
AB  - We have reported previously that the long-term survival of Mycobacterium 
      smegmatis is facilitated by a dual-active enzyme MSDGC-1 (renamed DcpA), which 
      controls the cellular turnover of cyclic diguanosine monophosphate (c-di-GMP). 
      Most mycobacterial species possess at least a single copy of a DcpA orthologue 
      that is highly conserved in terms of sequence similarity and domain architecture. 
      Here, we show that DcpA exists in monomeric and dimeric forms. The dimerization 
      of DcpA is due to non-covalent interactions between two protomers that are 
      arranged in a parallel orientation. The dimer shows both synthesis and hydrolysis 
      activities, whereas the monomer shows only hydrolysis activity. In addition, we 
      have shown that DcpA is associated with the cytoplasmic membrane and exhibits 
      heterogeneous cellular localization with a predominance at the cell poles. 
      Finally, we have also shown that DcpA is involved in the change in cell length 
      and colony morphology of M. smegmatis. Taken together, our study provides 
      additional evidence about the role of the bifunctional protein involved in 
      c-di-GMP signalling in M. smegmatis.
CI  - The Authors.
FAU - Sharma, Indra Mani
AU  - Sharma IM
AD  - Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
FAU - Prakash, Sunita
AU  - Prakash S
AD  - Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
FAU - Dhanaraman, Thillaivillalan
AU  - Dhanaraman T
AD  - Institute for Research in Immunology and Cancer, Universite de Montreal, Montreal 
      H3C 3J7, Quebec, Canada.
FAU - Chatterji, Dipankar
AU  - Chatterji D
AD  - Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140718
PL  - England
TA  - Microbiology (Reading)
JT  - Microbiology (Reading, England)
JID - 9430468
RN  - 0 (Escherichia coli Proteins)
RN  - 61093-23-0 (bis(3',5')-cyclic diguanylic acid)
RN  - EC 4.6.- (Phosphorus-Oxygen Lyases)
RN  - EC 4.6.1.- (diguanylate cyclase)
RN  - H2D2X058MU (Cyclic GMP)
SB  - IM
MH  - Cell Membrane/enzymology
MH  - Cyclic GMP/*analogs & derivatives/metabolism
MH  - Escherichia coli Proteins/*metabolism
MH  - Hydrolysis
MH  - Mycobacterium smegmatis/cytology/*enzymology/genetics/growth & development
MH  - Phosphorus-Oxygen Lyases/*metabolism
MH  - Protein Binding
MH  - *Protein Multimerization
EDAT- 2014/07/20 06:00
MHDA- 2015/06/04 06:00
CRDT- 2014/07/20 06:00
PHST- 2014/07/20 06:00 [entrez]
PHST- 2014/07/20 06:00 [pubmed]
PHST- 2015/06/04 06:00 [medline]
AID - 10.1099/mic.0.080200-0 [doi]
PST - ppublish
SO  - Microbiology (Reading). 2014 Oct;160(Pt 10):2304-2318. doi: 
      10.1099/mic.0.080200-0. Epub 2014 Jul 18.