Homopolymer length variation in the Drosophila gene mastermind

Runs of identical amino acids encoded by triplet repeats (homopolymers) are components of numerous proteins, yet their role is poorly understood. Large numbers of homopolymers are present in the Drosophila melanogaster mastermind (mam) protein surrounding several unique charged amino acid clusters....

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Bibliographic Details
Published in:Journal of molecular evolution 1993-11, Vol.37 (5), p.483-495
Main Authors: Newfeld, S.J, Schmid, A.T, Yedvobnick, B
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Biological and medical sciences
Chromosome Banding
CODE GENETIQUE
CODIGO GENETICO
Codon
Conserved Sequence
Drosophila
Drosophila - embryology
Drosophila - genetics
DROSOPHILA MELANOGASTER
Drosophila melanogaster - embryology
Drosophila melanogaster - genetics
Drosophila Proteins
Fundamental and applied biological sciences. Psychology
Genes, Insect - genetics
Genes. Genome
Genome
Insect Hormones - genetics
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Nuclear Proteins - genetics
POLIMEROS
POLYMERE
Polynucleotides - genetics
Repetitive Sequences, Nucleic Acid
Restriction Mapping
RNA, Messenger - isolation & purification
SECUENCIA NUCLEICA
Sequence Homology, Amino Acid
SEQUENCE NUCLEIQUE
TECHNIQUE ANALYTIQUE
TECNICAS ANALITICAS
Tissue Distribution
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Summary:Runs of identical amino acids encoded by triplet repeats (homopolymers) are components of numerous proteins, yet their role is poorly understood. Large numbers of homopolymers are present in the Drosophila melanogaster mastermind (mam) protein surrounding several unique charged amino acid clusters. Comparison of mam sequences from D. virilis and D. melanogaster reveals a high level of amino acid conservation in the charged clusters. In contrast, significant divergence is found in repetitive regions resulting from numerous amino acid replacements and large insertions and deletions. It appears that repetitive regions are under less selective pressure than unique regions, consistent with the idea that homopolymers act as flexible spacers separating functional domains in proteins. Notwithstanding extensive length variation in intervening homopolymers, there is extreme conservation of the amino acid spacing of specific charge clusters. The results support a model where homopolymer length variability is constrained by natural selection
ISSN:0022-2844
1432-1432
DOI:10.1007/BF00160429