Research Highlights

Howell lab deduces the mechanism of type IV pilus motors

5 May 2017|

Howell lab

The type IV pilus is a long and sturdy grappling hook that bacteria use to attach to a surface and then pull themselves closer to the surface. They are important for virulence in many pathogens, including those that cause cholera, gonorrhoea, food-borne diseases, and multi-drug resistant hospital acquired infections. The molecular mechanism of the motors involved in throwing out and pulling […]

New genetic disease discovered by Drs. Aleixo Muise and Walter Kahr

7 April 2017|

Two of Biochemistry’s professors, Drs. Aleixo Muise and Walter Kahr have discovered a brand new genetic disease through their research at the Hospital for Sick Children.

Their research article is published on Nature Communications.

Their story was also highlighted on the Hospital for Sick Children, CBC The National and CBC News Network, and the Globe and Mail websites:

http://www.sickkids.ca/AboutSickKids/Newsroom/Past-News/2017/SickKids-team-identifies-new-disease-solves-medical-mystery.html

http://www.cbc.ca/news/thenational/new-disease-discovered-1.4054061

[…]

Stagljar lab reveals new interactions among GPCRs

16 March 2017|

Using the modified membrane yeast two‐hybrid (MYTH) technology, researchers from the Stagljar lab mapped membrane protein interactions for clinically important G protein coupled receptors (GPCRs).

Read the full story on Faculty of Medicine website.

Read their paper on Molecular Systems Biology.

 

Researchers revisit the role of conformational dynamics and the protein ensemble in catalysis

21 February 2017|

Houry lab identifies a novel regulator of respiratory chain complexes

13 February 2017|

Graphical abstract_120616

An interaction between the respiratory enzyme fumarate reductase (Frd, also known as Complex II) and an ATPase has been identified in E. coli by the Houry lab. The research shows that the RavA ATPase, belonging to a poorly characterized but ubiquitous MoxR family of AAA+ ATPases, associates with the Frd respiratory enzyme through an adaptor, which the group named ViaA. […]

Legend: Dr. Broecker’s and Dr. Ernst’s paper was featured on the Feb 7 cover of Structure

Ernst Lab discover new way to crystallize membrane proteins

7 February 2017|

The laboratory of Dr. Oliver Ernst has used X-ray crystallography to determine the structure of a membrane protein that never left a lipid-bilayer environment (i.e., without the use of conventional detergents). The work, published in Structure and highlighted on the Journal’s cover, was led by postdoctoral fellow Dr. Jana Broecker. Polymer-bounded lipid nanodiscs were used to extract and purify membrane proteins with their surrounding lipids and allowed […]

After release into the host cell, translocated bacterial substrates (effectors) regulate one another through several different functional interactions: indirectly, through counteracting modification of a shared host target, or directly through either steric complex formation or direct modification of one effector by another.

Ensminger lab discovers a class of bacterial effectors with novel regulatory activities

3 February 2017|

Many bacterial pathogens modulate their hosts through complex arsenals of effector proteins that are injected into host cell during infection. Indeed, the concept that effectors target host proteins and processes to modulate their activities is central to the current molecular understanding of host-pathogen interactions. Legionella pneumophila, the causative agent of a deadly pneumonia known as Legionnaires’ disease, has over 300 effectors, which is the largest known arsenal amongst bacterial pathogens. […]

Mechanism of misfolded protein rescue.

Lingwood Lab discover new approach to rescue endogenous misfolded proteins

1 February 2017|

Newly made proteins which do not quite achieve the correct 3D shape in the ER are moved to the cell cytoplasm via a specific membrane pore, and broken down. Many disease causing gene mutations e.g. in cystic fibrosis, also result in misfolding of the mutant protein, and its transport though this pore, for cytoplasmic degradation. This pore is hijacked by some bacterial toxins which need to access the cytoplasm to […]

An artistic interpretation of the enzyme fluoroacetate dehalogenase binding substrate (green) in the left subunit and releasing bound water molecules (red) in the right-hand subunit.

The roles of protein dynamics and water networks in catalysis visualized

1 February 2017|

The dimeric enzyme fluoroacetate dehalogenase is one of only a handful of protein catalysts that can break the strongest bond in organic chemistry, the one between carbon and fluorine atoms, in the process transforming the highly toxic pesticide fluoroacetate into glycolate, a benign molecule.  The laboratories of Emil Pai and Scott Prosser, together with the group of Régis Pomès and collaborators in the US and Japan, have […]

Molecular Cell 2

Stagljar lab map interactions between receptor tyrosine kinases (RTKs) and protein tyrosine phosphatases (PTPs)

1 February 2017|

Featured on the front page of Molecular Cell, the research led by Dr. Igor Stagljar captured and mapped interactions between receptor tyrosine kinases (RTKs) and protein tyrosine phosphatases (PTPs) in human cells, leading to new and improved cancer therapies.

Read the full story on the Faculty of Medicine and The Varsity websites.

Davidson and Maxwell help discover off-switches for CRISPR

31 January 2017|

 

Featured on the cover of Cell, Biochemistry’s Dr. Alan Davidson and Dr. Karen Maxwell helped to discover how to turn off CRISPR. Read the full story.

Atomic model for the membrane-embedded motor of a eukaryotic V-ATPase

Proton pumping region of rotary ATPases revealed

3 November 2016|

In work led by postdoctoral fellow Mohammad T. Mazhab-Jafari, the Rubinstein laboratory used electron cryomicroscopy (cryo-EM) to determine the atomic structure of the membrane-bound region of a eukaryotic V-ATPase. This study, which was published in Nature, gives the first high-resolution structure for the membrane region of any rotary ATPase, a family of enzymes that includes proton pumping V-ATPases and proton-driven ATP synthases. The structure reveals several surprising features of […]