TY - JOUR
T1 - Facilitation of dissociation reaction of nucleotides bound to Mycobacterium tuberculosis DnaA
AU - Yamamoto, Kohji
AU - Moomey, Meredith
AU - Rajagopalan, Malini
AU - Madiraju, Murty V.V.S.
N1 - Funding Information:
Ichihashi and his colleagues (23) reported that the inhibitory effect of basic or neutral phospholipid on the interaction of acidic phospholipids with DnaA protein in E. coli. The biochemical findings suggest that DnaA activity is regulated by a change in the phospholipid composition of the cell membrane under physiological conditions. Although this may be an essential feature of the regulation of M. tuberculosis oriC replication, the nature of the rejuvenation of M. tuberculosis DnaA remains uncertain. Considering the complex nature of mycobacterial cell membranes, further studies are required to examine the effects of phospholipids on the regulation of DnaA activities This work was supported in part by grants from the National Institutes of Health to M.M. (AI41406) and M.R. (AI48417).
PY - 2008/6
Y1 - 2008/6
N2 - Acidic phospholipids have been shown to promote dissociation of bound nucleotides from Mycobacterium tuberculosis DnaA (DnaATB) purified under denaturing conditions [Yamamoto et al., (2002) Modulation of Mycobacterium tuberculosis DnaA protein-adenine-nucleotide interactions by acidic phospholipids. Biochem. J., 363, 305-311]. In the present study, we show that a majority of DnaATB in non-overproducing cells of M. tuberculosis is membrane associated. Estimation of phospholipid phosphorus following chloroform: methanol extraction of soluble DnaATB purified under native conditions (nDnaATB) confirmed the association with phospholipids. nDnaATB exhibited weak ATPase activity, and rapidly exchanged ATP for bound ADP in the absence of any added phospholipids. We suggest that the outcome of intra-cellular DnaATB-nucleotide interactions, hence DnaATB activity, is influenced by phospholipids.
AB - Acidic phospholipids have been shown to promote dissociation of bound nucleotides from Mycobacterium tuberculosis DnaA (DnaATB) purified under denaturing conditions [Yamamoto et al., (2002) Modulation of Mycobacterium tuberculosis DnaA protein-adenine-nucleotide interactions by acidic phospholipids. Biochem. J., 363, 305-311]. In the present study, we show that a majority of DnaATB in non-overproducing cells of M. tuberculosis is membrane associated. Estimation of phospholipid phosphorus following chloroform: methanol extraction of soluble DnaATB purified under native conditions (nDnaATB) confirmed the association with phospholipids. nDnaATB exhibited weak ATPase activity, and rapidly exchanged ATP for bound ADP in the absence of any added phospholipids. We suggest that the outcome of intra-cellular DnaATB-nucleotide interactions, hence DnaATB activity, is influenced by phospholipids.
UR - https://www.scopus.com/pages/publications/46349097501
UR - https://www.scopus.com/pages/publications/46349097501#tab=citedBy
U2 - 10.1093/jb/mvn025
DO - 10.1093/jb/mvn025
M3 - Article
C2 - 18296714
AN - SCOPUS:46349097501
SN - 0021-924X
VL - 143
SP - 759
EP - 764
JO - Journal of biochemistry
JF - Journal of biochemistry
IS - 6
ER -
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