DNA sequence encoding the amino-terminal region of the human c-src protein: implications of sequence divergence among src-type kinase oncogenes

We sequenced the 5'-coding region of the human c-src gene, exons 2 through 5, corresponding to one-third of the human c-src protein consisting of 536 amino acids. Sequence analysis of the src type of protein kinases revealed that the amino-terminal region encoded by exon 2 contains sequences specific for the src proteins and raised the possibility that this region is involved in the recognition of a src-specific substrate(s) or receptor(s).

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Organizational analysis of elav gene and functional analysis of ELAV protein of Drosophila melanogaster and Drosophila virilis.

Molecular and Cellular Biology ◽

10.1128/mcb.11.6.2994 ◽

1991 ◽

Vol 11 (6) ◽

pp. 2994-3000 ◽

Cited By ~ 15

Author(s):

K M Yao ◽

K White

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Rna Binding ◽

Terminal Region ◽

Drosophila Virilis ◽

Functional Domain ◽

Amino Terminal ◽

Binding Domains ◽

Rna Binding Domains

Drosophila virilis genomic DNA corresponding to the D. melanogaster embryonic lethal abnormal visual system (elav) locus was cloned. DNA sequence analysis of a 3.8-kb genomic piece allowed identification of (i) an open reading frame (ORF) with striking homology to the previously identified D. melanogaster ORF and (ii) 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% identity at the amino acid level, indicating a strong structural constraint for this functional domain. The amino-terminal region is 36 amino acids longer in D. virilis, and the conservation is 66%. In in vivo functional tests, the D. virilis ORF was indistinguishable from the D. melanogaster ORF. Furthermore, a D. melanogaster ORF encoding an ELAV protein with a 40-amino-acid deletion within the alanine/glutamine-rich region was also able to supply elav function in vivo. Thus, the divergence of the amino-terminal region of the ELAV protein reflects lowered functional constraint rather than species-specific functional specification.

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Amino Acids in the Amino Terminal Region of the Rat Prolactin Contribute to PRL-Receptor Binding and NB2 Cell Proliferation Activity

Biochemical and Biophysical Research Communications ◽

10.1006/bbrc.1994.2666 ◽

1994 ◽

Vol 205 (1) ◽

pp. 312-319 ◽

Cited By ~ 4

Author(s):

O. Maruyama ◽

T. Kato ◽

K. Wakabayashi ◽

Y. Kato

Keyword(s):

Amino Acids ◽

Cell Proliferation ◽

Receptor Binding ◽

Terminal Region ◽

Amino Terminal ◽

Cell Proliferation Activity ◽

Proliferation Activity

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The capsid protein of Semliki Forest virus has clusters of basic amino acids and prolines in its amino-terminal region.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.77.11.6376 ◽

1980 ◽

Vol 77 (11) ◽

pp. 6376-6380 ◽

Cited By ~ 53

Author(s):

H. Garoff ◽

A. M. Frischauf ◽

K. Simons ◽

H. Lehrach ◽

H. Delius

Keyword(s):

Amino Acids ◽

Capsid Protein ◽

Semliki Forest Virus ◽

Terminal Region ◽

Basic Amino Acids ◽

Amino Terminal

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Characterization of the mouse thyrotrophin-releasing hormone receptor gene: an exon corresponds to a deletion in the rat cDNA

Journal of Molecular Endocrinology ◽

10.1677/jme.0.0110141 ◽

1993 ◽

Vol 11 (2) ◽

pp. 141-149 ◽

Cited By ~ 6

Author(s):

S M Duthie ◽

P L Taylor ◽

K A Eidne

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Stop Codon ◽

Amino Acid Sequences ◽

R Gene ◽

Coding Region ◽

Thyrotrophin Releasing Hormone ◽

Exon 2 ◽

Exon 4

ABSTRACT The cloning and characterization of the mouse TRH receptor (TRH-R) gene revealed an untranslated exon (exon 1), a single intron and an upstream dinucleotide repeat sequence (d(TG)16.d(AG)21) in the 5′ untranslated region (UTR). The coding region was contained almost entirely on a second exon (exon 2), with the final amino acid and stop codon at the COOH terminus of the gene encoded by a third exon (exon 3) flanked by two introns. The 3′ UTR was contained on the remainder of exon 3 and on the final exon (exon 4). Exon 3 (228 bp) corresponds exactly to a 228 bp deletion that exists in the rat TRH-R cDNA, but not in the mouse cDNA. The mouse TRH-R cDNA encodes a protein of 393 amino acids which is 96% homologous to the rat TRH-R protein of 412 amino acids, but is 19 amino acids shorter at its COOH terminus. The coding sequence for these 19 amino acids (plus 1 extra amino acid) does exist in the mouse TRH-R gene, but the sequence is encoded by exon 4, separated from the rest of the coding region by the stop codon and 223 bp of 3′ UTR on exon 3. Splicing of exon 3 in the mouse TRH-R gene would remove the last amino acid, the stop codon and the 223 bp of 3′ UTR, allowing transcription to continue into the 3′ UTR on exon 4, which encodes the 19 extra amino acids found in the rat cDNA. This would then result in an alternative 412 amino acid version of the mouse TRH-R protein, with 95% homology to the rat TRH-R. This study focused on the structural differences in the intracellular COOH-terminal tail of the receptor, which is known to be a functionally important domain in other members of the G protein-coupled receptor family. We have also recently characterized the human TRH-R cDNA, which revealed a third variant at the COOH terminus. Comparisons between mouse, rat and human TRH-Rs show that the amino acid sequences are virtually identical. However, significant differences between these species exist at the COOH terminus, with each TRH-R having a unique form of the COOH-terminal tail, beginning at exactly the same site and encoding 1, 20 and 6 amino acids in the mouse, rat and human respectively.

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The structurally distinct form of pp60c-src detected in neuronal cells is encoded by a unique c-src mRNA

Molecular and Cellular Biology ◽

10.1128/mcb.7.11.4142-4145.1987 ◽

1987 ◽

Vol 7 (11) ◽

pp. 4142-4145

Author(s):

J B Levy ◽

T Dorai ◽

L H Wang ◽

J S Brugge

Keyword(s):

Amino Acids ◽

Sequence Analysis ◽

Cdna Clone ◽

Neuronal Cultures ◽

Embryonic Brain ◽

Distinct Form ◽

Src Gene ◽

Brain Cdna Library ◽

The Brain ◽

Base Pair Insertion

A cellular src (c-src) cDNA clone was isolated from a chicken embryonic brain cDNA library and characterized by DNA sequence analysis. Comparison with the published sequence of a chicken genomic c-src clone indicated that the brain cDNA clone contained an 18-base-pair insertion located between exons 3 and 4 of the c-src gene. The six amino acids encoded by the insertion caused an alteration in the electrophoretic mobility of the c-src gene product similar to that of the structurally distinct form of the src protein detected in neuronal cultures.

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Separate information required for nuclear and subnuclear localization: additional complexity in localizing an enzyme shared by mitochondria and nuclei.

Molecular and Cellular Biology ◽

10.1128/mcb.12.12.5652 ◽

1992 ◽

Vol 12 (12) ◽

pp. 5652-5658 ◽

Cited By ~ 38

Author(s):

A M Rose ◽

P B Joyce ◽

A K Hopper ◽

N C Martin

Keyword(s):

Amino Acids ◽

Nuclear Periphery ◽

Immunofluorescent Staining ◽

Coding Region ◽

Nuclear Targeting ◽

Subnuclear Localization ◽

Amino Terminal ◽

Linear Sequence ◽

Trna Methyltransferase ◽

Terminal Amino

The TRM1 gene of Saccharomyces cerevisiae codes for a tRNA modification enzyme, N2,N2-dimethylguanosine-specific tRNA methyltransferase (m2(2)Gtase), shared by mitochondria and nuclei. Immunofluorescent staining at the nuclear periphery demonstrates that m2(2)Gtase localizes at or near the nuclear membrane. In determining sequences necessary for targeting the enzyme to nuclei and mitochondria, we found that information required to deliver the enzyme to the nucleus is not sufficient for its correct subnuclear localization. We also determined that mislocalizing the enzyme from the nucleus to the cytoplasm does not destroy its biological function. This change in location was caused by altering a sequence similar to other known nuclear targeting signals (KKSKKKRC), suggesting that shared enzymes are likely to use the same import pathway as proteins that localize only to the nucleus. As with other well-characterized mitochondrial proteins, the mitochondrial import of the shared methyltransferase depends on amino-terminal amino acids, and removal of the first 48 amino acids prevents its import into mitochondria. While this truncated protein is still imported into nuclei, the immunofluorescent staining is uniform throughout rather than at the nuclear periphery, a staining pattern identical to that described for a fusion protein consisting of the first 213 amino acids of m2(2)Gtase in frame with beta-galactosidase. As both of these proteins together contain the entire m2(2)Gtase coding region, the information necessary for association with the nuclear periphery must be more complex than the short linear sequence necessary for nuclear localization.

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Organizational analysis of elav gene and functional analysis of ELAV protein of Drosophila melanogaster and Drosophila virilis

Molecular and Cellular Biology ◽

10.1128/mcb.11.6.2994-3000.1991 ◽

1991 ◽

Vol 11 (6) ◽

pp. 2994-3000

Author(s):

K M Yao ◽

K White

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Rna Binding ◽

Terminal Region ◽

Drosophila Virilis ◽

Functional Domain ◽

Amino Terminal ◽

Binding Domains ◽

Rna Binding Domains

Drosophila virilis genomic DNA corresponding to the D. melanogaster embryonic lethal abnormal visual system (elav) locus was cloned. DNA sequence analysis of a 3.8-kb genomic piece allowed identification of (i) an open reading frame (ORF) with striking homology to the previously identified D. melanogaster ORF and (ii) 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% identity at the amino acid level, indicating a strong structural constraint for this functional domain. The amino-terminal region is 36 amino acids longer in D. virilis, and the conservation is 66%. In in vivo functional tests, the D. virilis ORF was indistinguishable from the D. melanogaster ORF. Furthermore, a D. melanogaster ORF encoding an ELAV protein with a 40-amino-acid deletion within the alanine/glutamine-rich region was also able to supply elav function in vivo. Thus, the divergence of the amino-terminal region of the ELAV protein reflects lowered functional constraint rather than species-specific functional specification.

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