Literature DB >> 2981850

The structural organization of the chicken calmodulin gene.

R C Simmen, T Tanaka, K F Ts'ui, J A Putkey, M J Scott, E C Lai, A R Means.   

Abstract

The structural organization of the entire chicken calmodulin (CaM) gene was determined by analysis of overlapping genomic clones obtained from Charon 4A and cosmid DNA libraries. These clones together span 39 kilobases of chicken genomic DNA. The CaM gene is 12 kilobases long and contains 8 exons interrupted by introns of highly variable size. The first intron (A) is only 19 base pairs (bp) long and divides the 5' untranslated region. Intron B separates the ATG from the first nucleotide of the triplet which encodes the NH2-terminal amino acid of CaM (Ala) whereas intron C separates the triplets encoding amino acids 10-11. Introns D, F, and G interrupt the Ca2+ binding subdomains II, III, and IV of CaM whereas intron E is localized in the linker region between the highly homologous NH2- and COOH-terminal halves of the protein. Primer extension studies using chicken brain poly(A+) mRNA and a fragment from the 5' untranslated region of a CaM cDNA identified the presumptive transcription initiation site (cap site) of the mRNA to be 103 bp 5' from the initiation condon ATG. A consensus sequence TATTTAA was localized 29 bp 5' from this cap site while a CCAAT sequence was located further 5' at position -58 bp. The structure of the CaM gene is strikingly similar to genes that encode other Ca2+ binding proteins from sea urchin, chicken, rat, and quail. These data suggest a conservation of genome organization related to the calcium binding and regulatory domains of Ca2+ binding proteins.

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Year:  1985        PMID: 2981850

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  18 in total

1.  Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences.

Authors:  N D Moncrief; R H Kretsinger; M Goodman
Journal:  J Mol Evol       Date:  1990-06       Impact factor: 2.395

2.  Do exons code for structural or functional units in proteins?

Authors:  T W Traut
Journal:  Proc Natl Acad Sci U S A       Date:  1988-05       Impact factor: 11.205

3.  Gene organization of the small subunit of human calcium-activated neutral protease.

Authors:  S Miyake; Y Emori; K Suzuki
Journal:  Nucleic Acids Res       Date:  1986-11-25       Impact factor: 16.971

4.  Substitution at position 116 of Schizosaccharomyces pombe calmodulin decreases its stability under nitrogen starvation and results in a sporulation-deficient phenotype.

Authors:  T Takeda; Y Imai; M Yamamoto
Journal:  Proc Natl Acad Sci U S A       Date:  1989-12       Impact factor: 11.205

5.  The 5' splice site: phylogenetic evolution and variable geometry of association with U1RNA.

Authors:  M Jacob; H Gallinaro
Journal:  Nucleic Acids Res       Date:  1989-03-25       Impact factor: 16.971

6.  Structure of the chromosomal chicken progesterone receptor gene.

Authors:  C S Huckaby; O M Conneely; W G Beattie; A D Dobson; M J Tsai; B W O'Malley
Journal:  Proc Natl Acad Sci U S A       Date:  1987-12       Impact factor: 11.205

Review 7.  The myosin alkali light chain proteins and their genes.

Authors:  P J Barton; M E Buckingham
Journal:  Biochem J       Date:  1985-10-15       Impact factor: 3.857

8.  Structure of vertebrate genes: a statistical analysis implicating selection.

Authors:  M W Smith
Journal:  J Mol Evol       Date:  1988       Impact factor: 2.395

9.  Structure and nucleotide sequence of the rat intestinal vitamin D-dependent calcium binding protein gene.

Authors:  J Krisinger; H Darwish; N Maeda; H F DeLuca
Journal:  Proc Natl Acad Sci U S A       Date:  1988-12       Impact factor: 11.205

10.  Evolution of EF-hand calcium-modulated proteins. III. Exon sequences confirm most dendrograms based on protein sequences: calmodulin dendrograms show significant lack of parallelism.

Authors:  S Nakayama; R H Kretsinger
Journal:  J Mol Evol       Date:  1993-05       Impact factor: 2.395

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