A Study of the Interplay Between Saccharomyces Cerevisiae Transcription and DNA Repair

A Study of the Interplay Between Saccharomyces Cerevisiae Transcription and DNA Repair
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Total Pages : 268
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ISBN-10 : OCLC:828560808
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Book Synopsis A Study of the Interplay Between Saccharomyces Cerevisiae Transcription and DNA Repair by : Priyasri Shotton

Download or read book A Study of the Interplay Between Saccharomyces Cerevisiae Transcription and DNA Repair written by Priyasri Shotton and published by . This book was released on 2012 with total page 268 pages. Available in PDF, EPUB and Kindle. Book excerpt: DNA is the storehouse of genetic information for the normal functioning of all cellular processes. This DNA is "read" by RNA Polymerases (RNAP) to carry out the transcription process, which is one of the most vital regulatory mechanisms within the cell for gene expression. There are three important RNA Polymerases available in the cell. RNAPI synthesizes ribosomal RNAs, while RNAPII makes mRNA precursors, snRNAs and most microRNAs, additionally RNAPIII takes care of tRNAs, small RNAs and 5S rRNAs that occur in the nucleus and the cytosol. The work in the author's lab focuses on the function of RNAPII transcription. It is not straightforward for RNAPII to transcribe the DNA, it needs to struggle with two major roadblocks that are in its path. First, is the nucleosomal barrier that is scattered across the coding regions of active genes. The mechanism to overcome this major obstacle is a very complex process that involves an extensive range of proteins which work collectively to help in the alteration of chromatin structure that ultimately facilitates transcriptional regulation. In the thesis, the author has attempted to take a look at this intricate network and has studied the function of Rad26p, in yeast (associated with CSB-Cockayne syndrome B, in humans), a transcription coupled DNA repair factor, having an additional role in transcription. The results reveal that Rad26p plays a novel role in the regulation of elongation by modulating histone H2A-H2B dimer occupancy.


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