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Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations
Published on: November 7, 2019
Characterization of a full-length cDNA encoding a bovine four tandem-repeat ubiquitin
1Max-Planck-Institut für biophysikalische Chemie, Department of Molecular Biology, Göttingen, Germany.
Insights
Researchers identified two bovine ubiquitin clones from a seminal vesicle cDNA library. One clone showed a unique serine-to-phenylalanine substitution, potentially due to allelic polymorphism in ubiquitin gene expression.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Ubiquitin is a crucial protein involved in various cellular processes, including protein degradation and gene regulation.
- The bovine seminal vesicle is a source of genetic material for studying protein expression.
Purpose of the Study:
- To screen a bovine seminal vesicle cDNA library for ubiquitin-encoding clones.
- To analyze the sequence and identify any variations in the ubiquitin repeats.
Main Methods:
- Screening of a lambda gt11 cDNA library using monospecific anti-ubiquitin immunoglobulin Gs (IgGs).
- DNA sequencing and amino acid sequence analysis of isolated clones (pUF4AA and pUD4AA).
Main Results:
- Two independent clones, pUF4AA and pUD4AA, were isolated.
- pUF4AA contained a polyubiquitin coding region with four tandem repeats, featuring a serine to phenylalanine substitution at position 133 in the second repeat.
- pUD4AA exhibited the typical serine residue at position 133.
Conclusions:
- The identified serine-phenylalanine substitution in bovine ubiquitin may represent an allelic polymorphism.
- Further investigation is warranted to understand the functional implications of this variation in ubiquitin gene expression.
Abstract:
Screening of a bovine seminal vesicle cDNA library in lambda gt11 with monospecific anti-ubiquitin IgGs yielded two independent clones pUF4AA and pUD4AA. Sequence analysis of pUF4AA revealed a coding region for a polyubiquitin with four tandem-repeats. We observed a replacement of serine (133) by phenylalanine in the second ubiquitin repeat. The deduced amino acid sequence of pUD4AA, however, possessed the typical serine (133) residue. This serine-phenylalanine replacement could result from allelic polymorphism.
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