BEGIN:VCALENDAR
VERSION:2.0
PRODID:icalendar-ruby
CALSCALE:GREGORIAN
X-WR-CALNAME:Chemical Biology Seminar (Robert Silvers\, Florida State Unive
 rsity)
X-WR-TIMEZONE:Eastern Time (US & Canada)
BEGIN:VEVENT
DTSTAMP:20261006T034605Z
UID:tag:localist.com\,2008:EventInstance_50763519988739
DTSTART:20260302T210000Z
DTEND:20260302T220000Z
DESCRIPTION:Title:    “RNA binding of La-Related Proteins”\n\n \n\nAbst
 ract: \n\nLa-related proteins (LARPs) are a superfamily of RNA-binding pro
 teins characterized by the presence of a highly conserved domain known as 
 the La domain (LA). In the vast majority of LARPs\, this La domain forms t
 he La module in tandem with a downstream ribonucleotide recognition motif 
 (RRM). The archetypal La module found in LARP3 was the first to be discove
 red and demonstrates a specific recognition of nascent RNA polymerase III 
 (RNAP III) transcripts at their 3’ UUU-OH to impede digestion by exonucl
 eases. Other LARPs demonstrate similar function\, some evolving to contain
  other functional units to facilitate greater mRNA regulatory capacity.[1]
 \n\nHuman LARP6 (HsLARP6) plays a role in the post-transcriptional regulat
 ion of type I and III collagen biosynthesis and therefore plays an integra
 l part in onset and progression of fibrosis. Unlike most LARPs\, LARP6 spe
 cifically binds to a highly conserved double-stranded RNA structure\, the 
 5’ stem loop (5’SL)\, present in the mRNAs encoding type I and III col
 lagen. The 5’SL is 46-48 nucleotides in length and contains an internal 
 loop with 9 highly conserved nucleotides\, flanked by two stems with great
 er sequence variability. This 5’SL motif is conserved across all vertebr
 ates and is crucial for regulating the translation of these collagen mRNAs
 .\n\nRecently\, we have shown that 5'SL RNA binds via a unique\, previousl
 y undescribed binding site\, which we dubbed the noncanonical binding site
 .[2-4] While structurally similar to La domains of other LARPs\, the La do
 main of LARP6 features a unique basic patch that coincides with the noncan
 onical binding site. Furthermore\, the noncanonical interface enables the 
 La domain to discriminate 5’SL RNA from homopolymeric or purely helical 
 hairpin RNAs with low-nanomolar affinity\, overturning earlier views that 
 the adjacent RNA recognition motif is required for recognition.\n\n \n\nRe
 ferences\n\n1) Maraia et al. (2017) WIREs\, 8:e1430\n\n2) Gordon et al. (2
 025) Nucleic Acids Research\, 53\, gkaf682\n\n3) Gordon et al. (2025) Biom
 ol NMR Assign\, 19\, 165-17\n\n4) Gordon et al. (2025) ACS Omega\, 10\, 12
 699-12709
GEO:42.358262;-71.090045
LOCATION:Building 4\, Room 270
SUMMARY:Chemical Biology Seminar (Robert Silvers\, Florida State University
 )
URL;VALUE=URI:https://calendar.mit.edu/event/chemical-biology-seminar-rober
 t-silvers-florida-state-university
CATEGORIES:Conferences/Seminars/Lectures
END:VEVENT
END:VCALENDAR