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Modular multidomain phosphoryl transfer proteins of bacteria
1Department of Biology, University of California at San Diego, La Jolla, 92093-0116, USA. jreizer@ucad.edu
Current Opinion in Structural Biology
|June 1, 1997
Summary
Bacterial protein evolution frequently involves domain shuffling, including splicing, fusion, duplication, and deletion, particularly between protein domains. These evolutionary events are rare in other protein families, highlighting unique bacterial protein dynamics.
Area of Science:
- Molecular Biology
- Evolutionary Biology
- Biochemistry
Background:
- Multidomain phosphoryl transfer proteins are crucial in bacterial cellular processes.
- Understanding protein evolution requires analyzing domain dynamics.
Purpose of the Study:
- To investigate the frequency and patterns of evolutionary events in bacterial multidomain phosphoryl transfer proteins.
- To compare domain shuffling events in these proteins with other protein families.
Main Methods:
- Phylogenetic analysis of protein sequences.
- Structural analysis of protein domains.
- Comparative evolutionary analysis across protein superfamilies.
Main Results:
- Interdomain splicing, fusion, duplication, and deletion are frequent in bacterial phosphoryl transfer proteins.
- Intradomain events are rare.
- Domain shuffling is less common in other protein families.
Conclusions:
- Bacterial protein evolution exhibits a high propensity for domain shuffling, particularly interdomain events.
- These findings offer insights into the evolutionary mechanisms shaping bacterial proteomes.
- Examples include sugar phosphotransferase systems, signal transduction systems, and ABC transporters.