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Related Experiment Video

Updated: May 2, 2026

Creating Objects and Object Categories for Studying Perception and Perceptual Learning

Creating Objects and Object Categories for Studying Perception and Perceptual Learning

Published on: November 2, 2012

Architecture and metamorphosis.

Min Guo¹, Xiang-Lei Yang

¹Department of Cancer Biology, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL, 33410, USA, GuoMin@scripps.edu.

Topics in Current Chemistry

|March 29, 2013

Summary

This summary is machine-generated.

Aminoacyl-tRNA synthetases (aaRSs) in higher eukaryotes evolved new domains, expanding functions beyond protein synthesis. These domain additions contribute to complex biological roles and the multi-synthetase complex (MSC).

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Area of Science:

Molecular Biology
Evolutionary Biology
Biochemistry

Background:

Aminoacyl-tRNA synthetases (aaRSs) are essential enzymes for protein synthesis.
Compared to other housekeeping proteins, aaRSs exhibit a high propensity for acquiring new domains during evolution.
These domain additions correlate with increased biological complexity in higher eukaryotes.

Purpose of the Study:

To investigate the evolutionary expansion of aaRSs through the acquisition of new domains.
To characterize the origins, structures, and functions of these novel domains.
To explore the role of domain additions in the formation and function of the multi-synthetase complex (MSC) and non-canonical aaRS activities.

Main Methods:

Comparative analysis of protein domain evolution in aaRSs.
Sequence, structural, and functional characterization of aaRS domains.
Investigation of the assembly and composition of the human multi-synthetase complex (MSC).

Main Results:

aaRSs have acquired unique and common domain modules, some involved in nucleic acid binding and others in protein-protein interactions for MSC assembly.
The human MSC is a large complex (1.5 million Dalton) comprising nine aaRSs and three scaffold proteins.
Domain additions and functional expansions are widespread across aaRSs, leading to multi-functionality and diverse conformational states.

Conclusions:

The evolution of aaRSs in higher eukaryotes is characterized by domain additions that confer new biological functions beyond basic protein synthesis.
The multi-synthetase complex (MSC) plays a role in both protein synthesis and non-canonical functions.
Conformational changes in aaRSs, influenced by various mechanisms, are crucial for regulating their expanded functional repertoire in higher organisms.