<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-09-20T22:57:54Z</responseDate><request verb="GetRecord" identifier="oai:dspace.mit.edu:1721.1/108885" metadataPrefix="dim">https://dspace.mit.edu/server/oai/request</request><GetRecord><record><header><identifier>oai:dspace.mit.edu:1721.1/108885</identifier><datestamp>2026-06-16T18:14:31Z</datestamp><setSpec>com_1721.1_7582</setSpec><setSpec>com_1721.1_7581</setSpec><setSpec>col_1721.1_131022</setSpec></header><metadata><dim:dim xmlns:dim="http://www.dspace.org/xmlns/dspace/dim" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.dspace.org/xmlns/dspace/dim http://www.dspace.org/schema/dim.xsd">
   <dim:field mdschema="dc" element="contributor" qualifier="advisor" lang="en_US">Dennis H. Kim.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="author" lang="en_US">Cattie, Douglas J. (Douglas John)</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="other" lang="en_US">Massachusetts Institute of Technology. Department of Biology.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="department">Massachusetts Institute of Technology. Department of Biology</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="accessioned">2017-05-11T19:53:50Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="available">2017-05-11T19:53:50Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="copyright" lang="en_US">2016</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued" lang="en_US">2017</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="uri">http://hdl.handle.net/1721.1/108885</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="oclc" lang="en_US">986240171</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, February 2017.</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Cataloged from PDF version of thesis. "October 5, 2016."</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Includes bibliographical references.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en_US">The eukaryotic initiation factor 3 (elF3) is a protein complex composed of 13 subunits in mammals, and is an essential scaffold of the molecular interactions required for the formation of the 43S preinitiation complex (PIC). While these 13 subunits are broadly conserved within the eukaryotic phylogeny, both biochemical and evolutionary evidence suggests that translation initiation can proceed with a vastly reduced number of elF3 subunits, with as few as six subunits in the yeast species Saccharomyces cerevisiae. In this study, I report that homologs of eIF3 subunits elF3k and elF3I are nonessential in Caenorhabditis elegans, and that in their absence there is no defect in bulk protein translation. Surprisingly, mutants lacking these subunits exhibit both enhanced endoplasmic reticulum homeostasis and increased longevity, which implicates a potential regulatory role for these subunits in the maintenance of organismal physiology.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="statementofresponsibility" lang="en_US">by Douglas J. Cattie.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="degree" lang="en_US">Ph.D.</dim:field>
   <dim:field mdschema="dc" element="format" qualifier="extent" lang="en_US">139 pages</dim:field>
   <dim:field mdschema="dc" element="language" qualifier="iso" lang="en_US">eng</dim:field>
   <dim:field mdschema="dc" element="publisher" lang="en_US">Massachusetts Institute of Technology</dim:field>
   <dim:field mdschema="dc" element="rights" lang="en_US">MIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission.</dim:field>
   <dim:field mdschema="dc" element="rights" qualifier="uri" lang="en_US">http://dspace.mit.edu/handle/1721.1/7582</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en_US">Biology.</dim:field>
   <dim:field mdschema="dc" element="title" lang="en_US">Identifying a role for nonessential elF3 subunits eif-3.K and eif-3.L in the regulation of endoplasmic reticulum homeostasis and longevity in Caenorhabditis elegans</dim:field>
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   	&lt;Title>Identifying a role for nonessential elF3 subunits eif-3.K and eif-3.L in the regulation of endoplasmic reticulum homeostasis and longevity in Caenorhabditis elegans&lt;/Title>
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   	&lt;PublicationDate>2017&lt;/PublicationDate>
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        	&lt;DisplayName>Cattie, Douglas J. (Douglas John)&lt;/DisplayName>
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            &lt;DisplayName>Massachusetts Institute of Technology&lt;/DisplayName>
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    &lt;Keyword>Biology.&lt;/Keyword>
   	&lt;Abstract>The eukaryotic initiation factor 3 (elF3) is a protein complex composed of 13 subunits in mammals, and is an essential scaffold of the molecular interactions required for the formation of the 43S preinitiation complex (PIC). While these 13 subunits are broadly conserved within the eukaryotic phylogeny, both biochemical and evolutionary evidence suggests that translation initiation can proceed with a vastly reduced number of elF3 subunits, with as few as six subunits in the yeast species Saccharomyces cerevisiae. In this study, I report that homologs of eIF3 subunits elF3k and elF3I are nonessential in Caenorhabditis elegans, and that in their absence there is no defect in bulk protein translation. Surprisingly, mutants lacking these subunits exhibit both enhanced endoplasmic reticulum homeostasis and increased longevity, which implicates a potential regulatory role for these subunits in the maintenance of organismal physiology.&lt;/Abstract>
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