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Actin's prokaryotic homologs
1Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Box 800733, Charlottesville 22908-0733, USA. egelman@virginia.edu
Current Opinion in Structural Biology
|May 3, 2003
Summary
Prokaryotic homologs of actin, MreB and ParM, polymerize into filaments. Unlike highly conserved eukaryotic actin, bacterial actin homologs show less sequence similarity, suggesting evolutionary flexibility.
Area of Science:
- Biochemistry
- Molecular Biology
- Microbiology
Background:
- Actin is a highly conserved eukaryotic protein essential for cellular functions.
- Prokaryotic homologs, MreB and ParM, have been recently identified.
- MreB and ParM polymerize into filaments, influencing bacterial cell shape and plasmid segregation.
Purpose of the Study:
- To investigate the evolutionary conservation and sequence similarity of eukaryotic actin and its prokaryotic homologs.
- To understand the functional implications of sequence divergence between bacterial and eukaryotic actin-like proteins.
Main Methods:
- Sequence analysis of actin and its prokaryotic homologs (MreB, ParM).
- Comparative analysis of protein sequence identity and conservation patterns.
Main Results:
- Eukaryotic actins exhibit remarkable sequence conservation across species.
- Prokaryotic actin homologs (MreB and ParM) share only approximately 11% sequence identity with each other and with actin.
- Bacterial homologs show greater sequence divergence compared to eukaryotic actins.
Conclusions:
- The functional properties of eukaryotic F-actin may drive its high conservation.
- Bacterial actin homologs (MreB and ParM) have experienced fewer evolutionary constraints, leading to greater sequence diversity.
- Understanding these differences provides insights into the evolution of cytoskeletal proteins.