<?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>2026-09-18T21:56:00Z</responseDate><request verb="GetRecord" identifier="oai:dspace.mit.edu:1721.1/40962" metadataPrefix="dim">https://dspace.mit.edu/server/oai/request</request><GetRecord><record><header><identifier>oai:dspace.mit.edu:1721.1/40962</identifier><datestamp>2022-01-13T07:54:15Z</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">Tania A. Baker.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="author" lang="en_US">Schweidenback, Caterina Taiani Hill</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="other" lang="en_US">Massachusetts Institute of Technology. Dept. 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">2008-03-27T18:29:42Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="available">2008-03-27T18:29:42Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="copyright" lang="en_US">2007</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued" lang="en_US">2007</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="uri">http://hdl.handle.net/1721.1/40962</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="oclc" lang="en_US">213086838</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2007.</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">Transposable elements comprise a significant portion of both prokaryotic and eukaryotic genomes. These mobile segments of DNA have helped to shape the course of evolution by generating genetic mutations and contributing to genomic rearrangements. Transposable elements often target transposition to non-random DNA sites. Ideal target sites must be common, so as to ensure efficient propagation of the transposable element, and yet non-essential, so as to protect the host cell on which the element depends. Transposable elements have devised a plethora of strategies for targeting transposition to desirable DNA. This thesis investigates the molecular mechanisms involved in Mu transposition. We explore the interactions between the Mu transposase, MuA, and a Mu-encoded accessory protein, MuB. Together, these two proteins regulate Mu transposition and targeting. We demonstrate that MuB interacts with multiple subunits of the MuA transposase complex to stimulate transposition. These results corroborate previous theories that MuB acts as an allosteric regulator of MuA. We also investigate the mechanism by which Mu transposes into selected DNA. We find that MuB "delivers" favorable target DNA to the Mu transposase by tethering the DNA to MuA. This interaction is independent of ATP hydrolysis by MuB. The work described herein has contributed to our understanding of the protein-protein interactions involved in Mu transposition.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="statementofresponsibility" lang="en_US">by Caterina Taiani Hill Schweidenback.</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">101 p.</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">M.I.T. theses are protected by 
copyright. They may be viewed from this source for any purpose, but 
reproduction or distribution in any format is prohibited without written 
permission. See provided URL for inquiries about 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">Regulation of Mu transposition via communication between the transposase and Mu-encoded accessory protein</dim:field>
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   	&lt;Title>Regulation of Mu transposition via communication between the transposase and Mu-encoded accessory protein&lt;/Title>
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   	&lt;PublicationDate>2007&lt;/PublicationDate>
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        	&lt;DisplayName>Schweidenback, Caterina Taiani Hill&lt;/DisplayName>
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    &lt;Keyword>Biology.&lt;/Keyword>
   	&lt;Abstract>Transposable elements comprise a significant portion of both prokaryotic and eukaryotic genomes. These mobile segments of DNA have helped to shape the course of evolution by generating genetic mutations and contributing to genomic rearrangements. Transposable elements often target transposition to non-random DNA sites. Ideal target sites must be common, so as to ensure efficient propagation of the transposable element, and yet non-essential, so as to protect the host cell on which the element depends. Transposable elements have devised a plethora of strategies for targeting transposition to desirable DNA. This thesis investigates the molecular mechanisms involved in Mu transposition. We explore the interactions between the Mu transposase, MuA, and a Mu-encoded accessory protein, MuB. Together, these two proteins regulate Mu transposition and targeting. We demonstrate that MuB interacts with multiple subunits of the MuA transposase complex to stimulate transposition. These results corroborate previous theories that MuB acts as an allosteric regulator of MuA. We also investigate the mechanism by which Mu transposes into selected DNA. We find that MuB &amp;quot;delivers&amp;quot; favorable target DNA to the Mu transposase by tethering the DNA to MuA. This interaction is independent of ATP hydrolysis by MuB. The work described herein has contributed to our understanding of the protein-protein interactions involved in Mu transposition.&lt;/Abstract>
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