Bio:
I was born in Colombo, Sri Lanka, which is a tiny
island of the southern tip of India. After my stay in Germany I traveled
further west. Finally the journey ended in Parkhurst lab, where I
hope to be an expert in biophysical research.
I am married to Namali .Sheyenne is my daughter and
my son’s name is Devan .My hobbies are traveling, playing cricket,
learning foreign languages especially German and Sri Lankan traditional
music. After graduation I plan on working in the industry and I also
have a strong interest in teaching chemistry.
Current Research:
Since the discovery of DNA double helix by Watson
and Crick, significant progress has been made toward elucidation of
localized DNA structural variations and elements that impart the structural
variations. Localised double helix bending (curvature) is one of the
important feature in DNA structure. In addition to the significance
in the packaging in the nucleus, bending is associated with many biological
processes, including transcription, replication and recombination.
We are currently investigating a series of eleven 14 base pair oligonucleotides,
which bear variety of special elements such as full A-tract (A6),
partial A-tract (A3 and A4) and TATA element. Double labeled oligomers
are fluorescently labeled with TAMRA/FLURESCENE pair and XRODAMINE
/FLURESCENE pair. In the hope of improving our knowledge about duplex
curvature and flexibility in the solution we are currently measuring
the inter-dye distances and distance distribution of each duplex.
For this purpose time resolved fluorescence emission in conjunction
with fluorescence resonance energy transfer (FRET) is being used.
Previous Research - Protein Binding
Research:
Heterogeneous ribonucleoproteins (hnRNP) are very
abundant proteins found in the nucleus of all eukaryotes. Over 20
hnRNPS have been identified in mammalian systems. One of the most
abundant hnRNPs in vertebrates is hnRNPC.Studies on hnRNP C have shown
that the protein is involved in the packaging, splicing and nuclear
export of pre-mRNA.Recently, a new protein was discovered called p542
whose primary sequence was found to be highly similar to hnRNP C.
Individuals infected with Ebstein barr virus (EBV), the causative
agent of infectious mononucleosis, produce a auto-antibodies against
a p542, and auto-antibody production results from a common epitope
shared between one of the viral proteins and p542. In addition, sera
isolated from individuals with certain autoimmune disorders also contain
antibodies to p542. Thus, the molecular pathology of these disorders
probably results from inhibition of p542 function. The primary objective
of my research was to gain insight into the cellular activities of
p542, which is sharing some functional overlap with hnRNP C. Specifically,
in the studies reported here, Yeast Two-Hybrid assay has been utilized
to identify cellular proteins that interact with p542. In these experiments,
3.5 x 106 yeast colonies harboring a human cDNA library from brain
were screened for positive interactions with p542.Around 210 yeast
clones that are positive for containing human cDNA specified proteins
that interact with p542 have been identified. Of them positive clones
30 have been sequenced to identify the proteins that are interacting
with p542.One of the most frequently identified proteins was microtubule
associated protein 1 A (MAP 1A).MAP1A is an integral component of
the cytoskeleton architecture and recent studies show that it involve
in the attachment of the pre mRNA to the cytoskeleton. Association
of the p542 with the MAP1A may implicate p542 in the attachment of
pre mRNA to the cytoskeleton, pre mRNA trafficking and translation.
