Organizational analysis of elav gene and functional analysis of ELAV protein of Drosophila melanogaster and Drosophila virilis
- Brandeis Univ., Waltham, MA (United States)
Drosophila virilis genomic DNA corresponding analysis of a 3.8-kb genomic piece allowed identification of (1) an open reading frame (ORF) with striking homology to the previously identified D. melanogaster ORF and (2) conserved sequence elements of possible regulatory relevance within and flanking the second intron. Conceptual translation of the D. virilis ORF predicts a 519-amino-acid-long ribonucleoprotein consensus sequence-type protein. Similar to D. melanogaster ELAV protein, it contains three tandem RNA-binding domains and an alanine/glutamine-rich amino-terminal region. The sequence throughout the RNA-binding domains, comprising the carboxy-terminal 346 amino acids, shows an extraordinary 100% identify at the amino acid level, indicating a strong structural constraint for this functional domain. Thus, the divergence of the amino-terminal region of the ELAV protein reflects lowered functional constraint rather than species-specific functional specification.
- OSTI ID:
- 5145038
- Journal Information:
- Molecular and Cellular Biology; (United States), Vol. 11:6; ISSN 0270-7306
- Country of Publication:
- United States
- Language:
- English
Similar Records
[Studies of the repair of radiation-induced genetic damage in Drosophila]. Annual progress report, June 1, 1992--June 30, 1993
The molecular genetics of human diseases with defective DNA damage processing
Related Subjects
GENES
DNA SEQUENCING
NUCLEOPROTEINS
AMINO ACID SEQUENCE
ALANINES
BIOLOGICAL EVOLUTION
DROSOPHILA
GLUTAMIC ACID
NERVOUS SYSTEM
AMINO ACIDS
ANIMALS
ARTHROPODS
CARBOXYLIC ACIDS
DIPTERA
FLIES
FRUIT FLIES
INSECTS
INVERTEBRATES
MOLECULAR STRUCTURE
ORGANIC ACIDS
ORGANIC COMPOUNDS
PROTEINS
STRUCTURAL CHEMICAL ANALYSIS
550200* - Biochemistry