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Duplex (or quadruplet) CH domain containing human multidomain proteins: an inventory
1Howard University Medical School, Washington, DC, USA. ffriedberg@howard.edu
Molecular Biology Reports
|July 1, 2009
Summary
This study expands the catalog of human proteins with calponin homology (CH) domains, revealing evolutionary insights into their structure and origins. Gene duplication and exon shuffling are key mechanisms driving the evolution of these important multidomain proteins.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Genomics
Background:
- Calponin homology (CH) domains are actin-binding motifs found in various human multidomain proteins.
- Previous studies focused on singlet CH domain proteins, leaving duplex and quadruplet forms under-explored.
Purpose of the Study:
- To extend the inventory of human multidomain proteins to include those with duplex and quadruplet CH domains.
- To investigate the evolutionary origins and mechanisms driving the formation of these proteins.
Main Methods:
- Bioinformatic analysis of protein sequences to identify and categorize CH domain-containing proteins.
- Comparative genomics to trace the evolutionary history and gene duplication events.
Main Results:
- Identified several new duplex and one quadruplet CH domain-containing human proteins.
- Duplex CH domains are consistently located at the amino terminus of proteins.
- Amino acid conservation in connecting regions allowed grouping of 18 duplex proteins into six families based on recent gene duplication events.
Conclusions:
- Ancient multidomain proteins likely arose from exon shuffling, with CH domains placed at the amino end.
- Mechanisms like pseudogene formation, intragenomic duplications (slippage), and gene duplication with recombination contribute to the evolution of multidomain proteins.
- Gene duplication, modification, and domain recombination are significant evolutionary forces shaping multidomain protein architecture.
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