‘Tis the season to wish one another joy and love and peace . Happy holidays and a wonderful New Year! Biochemistry and Molecular Biology office will be closed for the holidays, from noon Tuesday, December 24, 2019 and will re-open Thursday, January 2, 2020.
Congratulations to the Undergraduate Biochemistry 3MT winners.
The Biochemistry and Molecular Biology department along with the BPP club hosted our 5th annual undergraduate biochemistry 3-minute thesis (3MT) event on November 20. Students who are currently in biochemistry directed studies (BIOC 448) or biochemistry honours thesis (BIOC 449) were invited to present the concept behind their research projects to an audience of undergraduate students and a panel of faculty judges. 2 people’s choice winners were selected by the audience and one winner was selected by the judging panel.
Ashley Yang., van Petegem Lab
Judging Panel Winner
Laura Meleady, Ciernia Lab
People’s Choice
An Te Chu, Jan Lab
Peoples Choice
Congratulations Biochemistry graduates!! UBC will be conferring Biochemistry degrees on Friday, November 29th at 9:00 a.m. in the Chan Centre. Fall 2019 schedule
“Prediction and Characterization of Protein-Protein Interfaces that Bind Intrinsically Disordered Protein Regions”, by Eric Wong, doctoral candidate, Gsponer Lab.
Thursday, November 28, 2019 12:30-3:30 pm, Room 203, Graduate Student Centre, 6371 Crescent Road.
Abstract:
Protein–protein interactions mediated by intrinsically disordered regions (IDRs) are differentiated from classical interactions between folded domains in terms of structure and function. Therefore, we developed a computational method specifically for the prediction of IDR-binding sites on the structures of folded domains. I will also discuss characteristics of IDR interactions, including localization patterns of disease and benign mutations that highlight the functional importance of IDR interactions.
“Prediction and Characterization of Protein-Protein Interfaces That Bind Intrinsically Disordered Protein Regions” , by Eric Wong, PhD Candidate, Gsponer Lab.
Protein–protein interactions mediated by intrinsically disordered regions (IDRs) are differentiated from classical interactions between folded domains in terms of structure and function. Therefore, we developed a computational method specifically for the prediction of IDR-binding sites on the structures of folded domains. I will also discuss characteristics of IDR interactions, including localization patterns of disease and benign mutations that highlight the functional importance of IDR interactions.
Monday, November 18, 2019 at 2:30 pm. LSC#3
Host: Dr. Joerg Gsponer
“Integrating protein biophysics and population dynamics to predict microbial evolution,” by Adrian Serohijos, Assistant Professor, Canada Research Chair in Evolutionary Biophysics & Population Dynamics, Department of Biochemistry, Université de Montréal.
“Evolution is a unifying theme in the urgent medical and public health problems we face today including cancer, the rise of antibiotic resistance, and the spread of pathogens. But the ability to predict evolution remains a major challenge because it requires bridging several scales of biological organization. Potential evolutionary pathways are determined by the “fitness landscape” (the genotype-phenotype relationship), but how this landscape is explored depends on population dynamics and ecology.
In the first half of the seminar, I describe our work where we showed that the fitness landscape of an RNA virus escaping a neutralizing antibody can be projected onto two biochemical traits, the capsid folding stability and its binding affinity to the antibody. We then developed a theory based on protein biophysics and population genetics to predict how the fitness landscape is dynamically explored. Using a droplet-based microfluidics “Evolution Chip”, we propagated millions of independent viral sub-populations, and showed that by tuning viral population size per drop, we could predict the direction of viral evolution. In the second half of the seminar, I will describe a chromosomal barcoding technique that allows simultaneous tracking of ~106 distinct cell lineages in an evolving bacterial population. We used this approach to study at high-resolution how microbial populations evolve under sub-inhibitory antibiotic concentrations.”
Monday, November 4, 2019 @2:30 pm, LSC #3
Host: Dr. Nobu Tokuriki
“Structural mechanisms of membrane fusion: from virus -cell to cell-cell”, presentation by Jeffrey Lee, Associate Professor, and Canada Research Chair, University of Toronto, Faculty of Medicine, Department of Laboratory Medicine and Pathobiology.
Monday, October 21, 2019 at 2:30 pm, LSC#3
Host: BMB Graduate Students.
“Human-yeast cross-species complementation of chromosome instability genes”, by Akil Hamza, doctoral candidate, Hieter Lab.
Monday, September 30, 2019 at 2:30 in LSC#3
Abstract
Humanized yeast offer a valuable resource with which to model and study human biology. Using cross-species complementation, model organisms like the budding yeast, Saccharomyces cerevisiae, can be utilized to measure the impact of tumor-specific mutations and screen for genetic vulnerabilities of genes overexpressed in cancer. To this end, we performed three parallel screens, one-to-one complementation screens for essential and nonessential yeast genes implicated in chromosome instability (CIN) and a pool-to-pool screen that queried all possible essential yeast genes for rescue of lethality by all possible human homologs. Our work identified 65 human cDNAs that can replace the null allele of essential yeast genes, including the nonorthologous pair yRFT1/hSEC61A1. For the nonessential yeast genes, 20 human-yeast complementation pairs were determined to be replaceable in 44 assays that test rescue of chemical sensitivity and/or CIN defects. For five human-yeast complementation pairs expressing human cDNAs encoding hLIG1, hSSRP1, hPPP1CA, hPPP1CC and hPPP2R1A, we introduced 45 tumor-specific missense mutations and assayed for growth defects and sensitivity to DNA-damaging agents in yeast. This set of human-yeast gene complementation pairs allows human genetic variants to be readily characterized in yeast, generating a prioritized list of somatic mutations that could contribute to chromosome instability in human tumors. We also selected a human-yeast pair expressing hFEN1, which is frequently overexpressed in cancer and is an anti-cancer therapeutic target, to perform synthetic dosage lethal (SDL) screens using ectopic overexpression of wild-type and catalytically inactive hFEN1 in yeast. The SDL screens identified homologous recombination (HR) repair mutants as synthetic lethal with overexpression of catalytically-inactive hFen1. The SDL interactions were dependent on binding of hFen1 to DNA suggesting that toxicity was a result of catalytically inactive hFen1 becoming trapped on DNA and resulting in DNA damage. Our study establishes the utility of using cross-species complementation and ectopic overexpression to generate human-yeast genetic interaction networks and to model protein-inhibitor interactions using genetic approaches. Overall, these data establish the utility of this cross-species experimental approach.
Congratulations Jason Read! 2019 Faculty of Medicine Award Recipient for Killam Teaching Prize. Each year, the Faculty of Medicine recognizes excellence in teaching. For this award category, nominees are from students, colleagues, and alumni in recognition of excellence in teaching.
Congratulations Dr. Shoukat Dedhar! 2019 Faculty of Medicine Award Recipient for UBC Killam Research Prize. This award is for a full-time faculty member in recognition of outstanding research and scholarly contributions.