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Comparative sequence analysis of the mRNAs coding for mouse and rat whey protein
Nucleic Acids Research
|June 25, 1982
Summary
Whey acidic protein (WAP) in mice and rats shows high conservation in its signal peptide and first cysteine domain. This suggests a crucial functional role for these regions and the 3' non-translated mRNA sequence.
Area of Science:
- Molecular Biology
- Comparative Genomics
- Biochemistry
Background:
- Whey acidic protein (WAP) is a significant milk protein in rodents.
- Understanding WAP evolution provides insights into mammalian lactation.
Purpose of the Study:
- To compare the sequences of mouse and rat WAP.
- To identify conserved regions and infer functional significance.
Main Methods:
- Cloning and sequencing of WAP cDNAs from mouse and rat.
- Deduction of amino acid sequences.
- Comparative sequence analysis of coding and non-coding regions.
Main Results:
- Mouse and rat WAP sequences were determined (134 and 137 amino acids).
- Proteins are acidic and cysteine-rich, with conserved N-terminal signal peptides and cysteine domains.
- Nucleotide sequence analysis revealed higher conservation in signal peptide and cysteine domain I.
- The 3' non-coding region exhibited significant conservation (91%).
Conclusions:
- The N-terminal signal peptide and first cysteine domain of WAP are highly conserved between mouse and rat.
- The 3' non-translated region of WAP mRNA may possess functional importance due to its low divergence rate.