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Concerted evolution in protists: Recent homogenization of a polyubiquitin gene in Trichomonas vaginalis

Concerted evolution in protists: Recent homogenization of a polyubiquitin gene in Trichomonas... Ubiquitin is a 76-amino-acid protein with a remarkably high degree of conservation between all known sequences. Ubiquitin genes are almost always multicopy in eukaryotes, and often are found as polyubiquitin genes—fused tandem repeats which are coexpressed. Seventeen ubiquitin sequences from the amitochondrial protist Trichomonas vaginalis have been examined here, including an 11-repeat fragment of a polyubiquitin gene. These sequences reveal a number of interesting features that are not seen in other eukaryotes. The predicted amino acid sequences lack several universally conserved residues, and individual units do not always encode identical peptides as is usually the case. On the nucleotide level, these repeats are in general highly variable, but one region in the polyubiquitin is extremely homogeneous, with seven repeats absolutely identical. Such extended stretches of homogeneity have never been observed in ubiquitin genes and since substitutions are common in other coding units, it is likely that these repeats are the product of a very recent homogenization or amplification. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Molecular Evolution Springer Journals

Concerted evolution in protists: Recent homogenization of a polyubiquitin gene in Trichomonas vaginalis

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References (45)

Publisher
Springer Journals
Copyright
Copyright © 1995 by Springer-Verlag New York Inc
Subject
Life Sciences; Evolutionary Biology; Microbiology; Plant Sciences; Plant Genetics and Genomics; Animal Genetics and Genomics; Cell Biology
ISSN
0022-2844
eISSN
1432-1432
DOI
10.1007/BF00175813
Publisher site
See Article on Publisher Site

Abstract

Ubiquitin is a 76-amino-acid protein with a remarkably high degree of conservation between all known sequences. Ubiquitin genes are almost always multicopy in eukaryotes, and often are found as polyubiquitin genes—fused tandem repeats which are coexpressed. Seventeen ubiquitin sequences from the amitochondrial protist Trichomonas vaginalis have been examined here, including an 11-repeat fragment of a polyubiquitin gene. These sequences reveal a number of interesting features that are not seen in other eukaryotes. The predicted amino acid sequences lack several universally conserved residues, and individual units do not always encode identical peptides as is usually the case. On the nucleotide level, these repeats are in general highly variable, but one region in the polyubiquitin is extremely homogeneous, with seven repeats absolutely identical. Such extended stretches of homogeneity have never been observed in ubiquitin genes and since substitutions are common in other coding units, it is likely that these repeats are the product of a very recent homogenization or amplification.

Journal

Journal of Molecular Evolution – Springer Journals

Published: Jul 5, 2004

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