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SGA screen identifies a cytoplasmic role for Dbp5/Rat8 and a novel player in nuclear pore complex biogenesis.

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Call No.	QH601.2 .S33 2007
Author	Scarcelli, John J.
Title	SGA screen identifies a cytoplasmic role for Dbp5/Rat8 and a novel player in nuclear pore complex biogenesis.
Date	2007
Abstract	The coordination and coupling of the several steps in mRNA biogenesis helps to ensure proper regulation of gene expression. The DEAD-box helicase Dbp5/Rat8 is an essential mRNA export factor that has also been implicated in other steps of mRNA biogenesis, from early in transcription to translation termination. In order to gain a better understanding of Dbp5/Rat8 function, we carried out a synthetic genetic array analysis of a strain harboring the rat8-2 mutation. Work in this thesis characterizes two different synthetic interactions detected via the SGA screen, between rat8-2 and the non-essential genes coding for proteins in the 5' to 3' cytoplasmic mRNA degradation machinery, and with the integral membrane protein Apq12. Several proteins functioning in cytoplasmic mRNA degradation localize to cytoplasmic foci termed processing bodies (P-bodies). Rat8/Dbp5 interacts functionally with P-body components. Like P-bodies, mutant rat8-2 protein localizes to cytoplasmic, mRNA dependent foci. These foci can contain several other mRNA export factors, such as Mex67, Mtr2, and Pab1 under certain genetic conditions. While these foci are distinct from P-bodies, they colocalize with P-bodies during heat stress. mRNA binding proteins such as Pub1 and Pab1, as well as Dbp5/Rat8 localize in these foci during heat stress regardless of genetic background. In higher eukaryotes, the mammalian forms of these proteins localize to stress granules during heat shock. Apq12 is an integral membrane protein of the nuclear envelope and endoplasmic reticulum. Cells lacking Apq12 are cold sensitive for growth, and a subset of nucleoporins, primarily those located asymmetrically at the cytoplasmic fibrils of the NPC, mislocalize to the cytoplasm. Electron microscopy indicates that deletion of APQ12 also caused defects in nuclear envelope (NE) morphology. Interestingly, low levels of benzyl alcohol, which increases the fluidity of membranes, prevented nucleoporin mislocalization and restored proper localization of nups that had accumulated in cytoplasmic foci upon a shift to lower temperature. Over-expression of the integral membrane protein Brr6 can correct the apq12 Δ-associated defects. Apq12 thus connects nuclear pore biogenesis to the dynamics of the NE.
Description	xii, 195 leaves : ill. 28 cm.
Format	application/pdf
Advisor	Charles K. Barlowe
Subject	Nuclear membranes. Membrane proteins. Genetic regulation.
College	Dartmouth Medical School -- Department of Biochemistry.
Issuing Body	Dartmouth Dissertations are made available through the Dartmouth Digital Library.
Degree	Thesis (Ph.D.)--Dartmouth College.
Copyright	All rights reserved. No part of this book may be reproduced in any form by any electronic or mechanical means without permission in writing from the author.
DOI	http://dx.doi.org/10.1349/ddlp.144

Title	Page 1
Format	application/pdf
Issuing Body	Dartmouth Dissertations are made available through the Dartmouth Digital Library.
Degree	Thesis (Ph.D.)--Dartmouth College.
Full Text	SGA screen identifies a cytoplasmic role for Dbp5/Rat8 and a novel player in nuclear pore complex biogenesis A Thesis Submitted to the Faculty in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biochemistry by John Scarcelli DARTMOUTH COLLEGE Hanover, New Hampshire August 20th, 2007 Examining Committee: ______________________________ Charles K. Barlowe, Ph.D. (chair) ___________________________ Lawrence C. Myers, Ph.D. ___________________________ David C. Amberg, Ph.D. ______________________________ Charles N. Cole, Ph.D. __________________________ Charles K. Barlowe, Ph.D. Dean of Graduate Studies

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SGA screen identifies a cytoplasmic role for Dbp5/Rat8 and a novel player in nuclear pore complex biogenesis.

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