Articles written in Journal of Biosciences
Volume 19 Issue 1 March 1994 pp 1-8
DNA primase from yeast mitochondria was shown to have a molecular weight of 67 kDa by SDS-PAGE and an S value of 5.5. It was shown to have preference for SS mitochondrial DNA especially fragments containing origins of replication, as a template to initiate DNA replication. Further examination of the enzyme showed its possible association with a ribonucleotide moiety essential for enzyme activity.
Volume 22 Issue 2 March 1997 pp 149-159
Yeast mitochondrial RNA polymerase was purified and resolved into 2 distinct fractions. Peak A was found to be nonspecific and exhibited characteristics of the core polymerase, whereas peak B exhibited characteristics of the holoenzyme.
Volume 22 Issue 5 December 1997 pp 567-573
Phosphorylation of endogeneous phosholipids of rat liver mitochondrial fractions with γ[32P]ATP revealed formation of all the known inositol phospholipids, such as phosphatidylinositol, phosphatidylinositol phosphate and phosphatidylinositol bisphosphate. Additionally, a new inositol phospholipid was detected. Incorporation of [3H]-labelled insositol followed a similar profile. Enzymatic experiments indicated that the new lipid could possibly be phosphatidylinositol trisphosphate. The presence of phosphoinositides-generated second messengers such as diacylglycerol and inositol trisphosphate was also confirmed. Protein kinase C, which acts as mediator between second messengers and nuclear factors, was also found to be present in mitochondria in significant amount. These results suggest that phosphoinositide signal transduction pathway is operative in rat liver mitochondria.