BEGIN:VCALENDAR

VERSION:2.0

PRODID:-//wp-events-plugin.com//7.2.2.1//EN

TZID:Asia/Jerusalem

X-WR-TIMEZONE:Asia/Jerusalem
BEGIN:VEVENT

UID:939@biology.technion.ac.il

DTSTART;TZID=Asia/Jerusalem:20210113T130000

DTEND;TZID=Asia/Jerusalem:20210113T140000

DTSTAMP:20210802T125903Z

URL:https://biology.technion.ac.il/en/seminars/ph-d-graduate-seminar-hadee
 l-khamis-2/

SUMMARY:Ph.D. Graduate Seminar-Hadeel Khamis [No Categories]
DESCRIPTION:Location:   \n Affiliation: \n Host:\n TitleA single molecule s
 tudy of protein-DNAinteractionsAbstract Bindingof transcription factors (T
 Fs) to regulatory regions in the genome is crucialfor the initiation of tr
 anscription\, and thus one of the most important layersin the regulation o
 f gene expression. Most TFs regulate multiple genes andinduce responses th
 at are gene-specific and vary between cell types anddevelopmental stages\,
  suggesting that the mere binding of the TF to the DNAcannot explain this 
 diversity of outcomes. In our work\, we developed a set ofnovel optical tw
 eezers assays to study how binding of Egr1\, a TF harboring 3zinc finger m
 otifs\, is tuned by variations in the binding site sequence\,sequences fla
 nking the binding site\, DNA methylation and the structure ofchromatin. Ou
 r results show that Egr1 binds to a “consensus” binding site in avery 
 stable conformation\, but variations in the core-site\, as observed invivo
 \,weaken the protein-DNA interactions\, resulting in a wide spectrum of st
 ructuresand binding energies\, that are also sensitive to variations in th
 e flankingsequences. Moreover\, we found that DNA methylation at the bindi
 ng sitesignificantly affects the affinity of the protein and the kinetics 
 of binding\,in a sequence- and position-specific manner. Methylation chang
 es the breathingkinetics of the DNA itself\, suggesting that the methylati
 on effect on Egr1binding is mediated by local structural changes in the DN
 A. Finally\, we studiedEgr1 binding in the vicinity of a nucleosome that c
 overs the binding site. Wefound that incorporation of the histone variant 
 H2A.Z resulted in an increasein nucleosome diffusion\, which increased Egr
 1 binding. Together\, our findingsreveal novel regulatory mechanisms to fi
 ne-tune the expression of genes.   

END:VEVENT

BEGIN:VTIMEZONE

TZID:Asia/Jerusalem

X-LIC-LOCATION:Asia/Jerusalem

BEGIN:STANDARD

DTSTART:20201025T010000

TZOFFSETFROM:+0300

TZOFFSETTO:+0200

TZNAME:IST

END:STANDARD

END:VTIMEZONE
END:VCALENDAR