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DTSTART:20251026T030000
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UID:20190528T091500UTC-fabaaa@http://www.ucmr.umu.se/
DTSTAMP:20260522T024722Z
CATEGORIES:Seminar
DESCRIPTION:<p>Department of Molecular Biology/MIMS<br />Extra Seminar</p>
 \n<p>Speaker:<br /><strong>Himanshu Sharma<br /></strong>Indian Institute 
 of Technology Guwahati\, Assam\, India</p>\n<p>Title:<br /><strong>Ribosom
 e assembly defects abrogate initiation factor mediated inspection of start
  codon</strong></p>\n<p>Host:<br />Jonas Barandun\, MIMS group leader and 
 SciLifeLab National Fellow\, Department of Molecular Biology</p>\n<p>Room:
  Thymine\, Dept Molecular Biology\, NUS\, bldg 6K/L 2 stairs up</p>\n<p><s
 trong>Abstract:</strong><br />Faithful protein synthesis is ensured by ext
 ensive quality control checkpoints using components of the translational m
 achinery. However\, the implications of defective ribosome assembly on pro
 tein synthesis and the associated translation quality control mechanisms i
 n bacteria remain grossly unaddressed. In this study\, using E. coli as a 
 model organism we show that premature ribosomes evade scrutiny of cognate 
 start Codon by initiation factors during translation initiation. Resultant
 ly the defective ribosomes make way into the translation cycle with severe
 ly compromised decoding and protein synthesis capabilities. The enfeebled 
 binding of premature ribosomes to initiation factors also licenses the rap
 id conversion of the 30S (pre) initiation complex to 70S initiation comple
 x. Overall\, our work highlights that a mass balance deficit between prema
 ture ribosomes and initiation factors steers the entry of premature riboso
 mes into the translation cycle.<br />(Co-Author: B. Anand)</p>
DTSTART;TZID=Europe/Stockholm:20190528T111500
DTEND;TZID=Europe/Stockholm:20190528T121500
SUMMARY:Ribosome assembly defects abrogate initiation factor mediated inspe
 ction of start codon
URL:http://www.ucmr.umu.se/about-ucmr/events/162-ucmr-calendar/164-seminar/
 578-ribosome-assembly-defects-abrogate-initiation-factor-mediated-inspecti
 on-of-start-codon.html
X-ALT-DESC;FMTTYPE=TEXT/HTML:<p>Department of Molecular Biology/MIMS<br />E
 xtra Seminar</p>\n<p>Speaker:<br /><strong>Himanshu Sharma<br /></strong>I
 ndian Institute of Technology Guwahati\, Assam\, India</p>\n<p>Title:<br /
 ><strong>Ribosome assembly defects abrogate initiation factor mediated ins
 pection of start codon</strong></p>\n<p>Host:<br />Jonas Barandun\, MIMS g
 roup leader and SciLifeLab National Fellow\, Department of Molecular Biolo
 gy</p>\n<p>Room: Thymine\, Dept Molecular Biology\, NUS\, bldg 6K/L 2 stai
 rs up</p>\n<p><strong>Abstract:</strong><br />Faithful protein synthesis i
 s ensured by extensive quality control checkpoints using components of the
  translational machinery. However\, the implications of defective ribosome
  assembly on protein synthesis and the associated translation quality cont
 rol mechanisms in bacteria remain grossly unaddressed. In this study\, usi
 ng E. coli as a model organism we show that premature ribosomes evade scru
 tiny of cognate start Codon by initiation factors during translation initi
 ation. Resultantly the defective ribosomes make way into the translation c
 ycle with severely compromised decoding and protein synthesis capabilities
 . The enfeebled binding of premature ribosomes to initiation factors also 
 licenses the rapid conversion of the 30S (pre) initiation complex to 70S i
 nitiation complex. Overall\, our work highlights that a mass balance defic
 it between premature ribosomes and initiation factors steers the entry of 
 premature ribosomes into the translation cycle.<br />(Co-Author: B. Anand)
 </p>
END:VEVENT
BEGIN:VEVENT
UID:20190529T113000UTC-5e80d8@http://www.ucmr.umu.se/
DTSTAMP:20260522T024722Z
CATEGORIES:Seminar
DESCRIPTION:<p><strong>Department of Molecular Biology/MIMS</strong><br />E
 xtra Seminar</p>\n<p><strong>Magnus Ölander</strong><br />Department of Ph
 armacy\, Uppsala University<br />Title:<br /><strong>Proteomic and functio
 nal analysis of </strong><br /><strong><em>in vitro</em> systems for studi
 es of drug disposition in the human small intestine and liver</strong></p>
 \n<p><br />Place: Thymine\, Molecular Biology bldg. 6K/L (2 stairs up)</p>
 \n<p>Host: Barbara Sixt\, MIMS group leader\,&nbsp\; Dept of Molecular Bio
 logy</p>\n<p>&nbsp\;</p>
DTSTART;TZID=Europe/Stockholm:20190529T133000
DTEND;TZID=Europe/Stockholm:20190529T143000
SUMMARY:Proteomic and functional analysis of in vitro systems for studies o
 f drug disposition in the human small intestine and liver
URL:http://www.ucmr.umu.se/about-ucmr/events/162-ucmr-calendar/164-seminar/
 579-proteomic-and-functional-analysis-of-in-vitro-systems-for-studies-of-d
 rug-disposition-in-the-human-small-intestine-and-liver.html
X-ALT-DESC;FMTTYPE=TEXT/HTML:<p><strong>Department of Molecular Biology/MIM
 S</strong><br />Extra Seminar</p>\n<p><strong>Magnus Ölander</strong><br /
 >Department of Pharmacy\, Uppsala University<br />Title:<br /><strong>Prot
 eomic and functional analysis of </strong><br /><strong><em>in vitro</em> 
 systems for studies of drug disposition in the human small intestine and l
 iver</strong></p>\n<p><br />Place: Thymine\, Molecular Biology bldg. 6K/L 
 (2 stairs up)</p>\n<p>Host: Barbara Sixt\, MIMS group leader\,&nbsp\; Dept
  of Molecular Biology</p>\n<p>&nbsp\;</p>
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