Structural and functional analysis of the NusB-S10 complex shared between transcription and translation

Luo, Xiao

dc.contributor.advisor	Wahl, Markus Prof. Dr.	de
dc.contributor.author	Luo, Xiao	de
dc.date.accessioned	2010-06-07T06:54:04Z	de
dc.date.accessioned	2013-01-18T14:28:57Z	de
dc.date.available	2013-01-30T23:50:19Z	de
dc.date.issued	2010-06-07	de
dc.identifier.uri	http://hdl.handle.net/11858/00-1735-0000-0006-B511-3	de
dc.identifier.uri	http://dx.doi.org/10.53846/goediss-3304
dc.format.mimetype	application/pdf	de
dc.language.iso	eng	de
dc.rights.uri	http://creativecommons.org/licenses/by-nc-nd/3.0/	de
dc.title	Structural and functional analysis of the NusB-S10 complex shared between transcription and translation	de
dc.type	doctoralThesis	de
dc.contributor.referee	Ficner, Ralf Prof. Dr.	de
dc.date.examination	2010-05-21	de
dc.subject.dnb	500 Naturwissenschaften	de
dc.description.abstracteng	Transcription and translation are two highly coupled processes during prokaryotic gene expression where ribosomes initiate translation on mRNAs already during transcription, in contrast to eukaryotes where two principle processes occur in two different cellular compartments. One of mechanisms by which transcription and translation in prokaryotes communicate directly with one other is sharing proteins, which have dual activity. As one such example, S10 protein was initially defined as a ribosomal (r-) protein before an additional role in transcription was discovered. S10 is a component of the 30S ribosomal subunit and participates together with NusB protein in processive transcription antitermination. NusB is implicated in translation through studies of its mutations that slow down the translation elongation rate. However, the exact role of NusB in translation remains unknown and the molecular mechanisms by which S10 and NusB can act as transcription or translation factors are still a mystery. Here, regions of S10 dispensable for transcription antitermination were delineated through complementation assays and recombineering. The crystal structure of a transcriptionally active NusB-S10 complex was determined. In the complex, S10 adopts the same fold as in the 30S subunit and is blocked from simultaneous association with the ribosome. Mass spectrometric mapping of UV-induced crosslinks revealed that the NusB-S10 complex presents an intermolecular, composite, and contiguous binding surface for RNAs containing BoxA antitermination signals. Furthermore, S10 overproduction complemented a nusB null phenotype. These data demonstrate that S10 and NusB together form a BoxA binding module, that NusB facilitates entry of S10 into the transcription machinery, and that S10 represents a central hub in processive antitermination. Last, the evidence that NusB plays a role of a loading factor in delivering S10 into transcription antitermination complex and into other molecular environment in vitro (crystals) allowed me to deduce a hypothesis that in translation NusB may still function as a loading factor that delivers S10 into ribosomes.	de
dc.contributor.coReferee	Fasshauer, Dirk Prof. Dr.	de
dc.subject.topic	Molecular Biology & Neurosciences Program	de
dc.subject.eng	antitermination	de
dc.subject.eng	Crystallography	de
dc.subject.eng	Ribosomes	de
dc.subject.bk	42.13	de
dc.identifier.urn	urn:nbn:de:gbv:7-webdoc-2487-9	de
dc.identifier.purl	webdoc-2487	de
dc.affiliation.institute	Göttinger Graduiertenschule für Neurowissenschaften und molekulare Biowissenschaften (GGNB)	de
dc.subject.gokfull	WF 200: Molekularbiologie	de
dc.identifier.ppn	636385159	de

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GGNB - Göttinger Graduiertenzentrum für Neurowissenschaften, Biophysik und molekulare Biowissenschaften [1114]
GGNB - Göttingen Graduate Center for Neurosciences, Biophysics and Molecular Biosciences

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