Forthcoming Events
Evolutionary analysis of proteins and biological pathways
Dr. Gurmeet Kaur, National Institutes of Health (NIH), USA and Corteva Agriscience, USA
Location : Online
Abstract: Understanding the intricate relationships between sequence, structure, and function is crucial for unraveling the mysteries of evolution of proteins and biological pathways. Leveraging high-throughput proteomic data analytics and comparative genomics tools, my research aims to illuminate fundamental principles regulating living systems while generating experimentally testable hypotheses. Through my continuing research in the field, I have been able to contribute to the advancement of the current understanding of two significant biological phenomena, viz., enzyme evolution and programmed cell death.
Have you ever wondered about the origin of enzymatic proteins? With a handful of supporting examples, it has been shown that non-catalytic proteins transition into functional enzymes during evolution. In one of my research studies, I investigated the emergence of a novel enzyme, organomercurial lyase (MerB). The latter has a peculiar enzymatic activity and proposed to have a novel protein fold. I showed that MerB, though structurally-unique, has emerged from the duplication and fusion of a simpler protein fold, the treble clef-like zinc finger fold. The emergence of a new structural scaffold was accompanied by repurposing of a part of a metal-binding pocket of the zinc finger into a novel enzymatic site. Thus, MerB serves as an elegant example to show how evolutionary forces drive the emergence of new biomolecules and biomolecular pathways.
In another fascinating study, we found the presence of animal apoptosis-like immunity mechanisms in bacteria. We revealed novel, highly-regulated chaperone-based systems that are used as survival tactics by prokaryotes with complex lifecycles. These architecturally-analogous systems have constant core modules coupled with highly-variable effector modules which is reminiscent of known biological conflict systems and co-evolutionary arms race. We also trace the provenance of key adaptor domains of metazoan apoptotic systems, namely those of the Death-like and TRADD-N superfamilies to multicellular bacteria. This underscores the similar operational “grammar” and shared “vocabulary” of protein domains in sensing and limiting infections during the multiple emergences of multicellularity across the tree of life.
My talk shall primarily focus on these two studies, and also outline my future research directions, hopefully fostering an engaging dialogue on these captivating topics.
Meeting ID: 929 8828 7425
Passcode: 583321
Have you ever wondered about the origin of enzymatic proteins? With a handful of supporting examples, it has been shown that non-catalytic proteins transition into functional enzymes during evolution. In one of my research studies, I investigated the emergence of a novel enzyme, organomercurial lyase (MerB). The latter has a peculiar enzymatic activity and proposed to have a novel protein fold. I showed that MerB, though structurally-unique, has emerged from the duplication and fusion of a simpler protein fold, the treble clef-like zinc finger fold. The emergence of a new structural scaffold was accompanied by repurposing of a part of a metal-binding pocket of the zinc finger into a novel enzymatic site. Thus, MerB serves as an elegant example to show how evolutionary forces drive the emergence of new biomolecules and biomolecular pathways.
In another fascinating study, we found the presence of animal apoptosis-like immunity mechanisms in bacteria. We revealed novel, highly-regulated chaperone-based systems that are used as survival tactics by prokaryotes with complex lifecycles. These architecturally-analogous systems have constant core modules coupled with highly-variable effector modules which is reminiscent of known biological conflict systems and co-evolutionary arms race. We also trace the provenance of key adaptor domains of metazoan apoptotic systems, namely those of the Death-like and TRADD-N superfamilies to multicellular bacteria. This underscores the similar operational “grammar” and shared “vocabulary” of protein domains in sensing and limiting infections during the multiple emergences of multicellularity across the tree of life.
My talk shall primarily focus on these two studies, and also outline my future research directions, hopefully fostering an engaging dialogue on these captivating topics.
Meeting ID: 929 8828 7425
Passcode: 583321