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  • Amino Acid Sequence  (3)
  • American Association for the Advancement of Science (AAAS)  (3)
  • 1985-1989  (2)
  • 1980-1984  (1)
  • 1950-1954
  • 1
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    Phase variation: evolution of a controlling element (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-19
    Description: Phase variation in bacteria is regulated by homologous recombination at a specific DNA site. This recombinational event causes the inversion of a 970-base-pair DNA sequence that includes the promoter necessary for transcription of a flagellar gene. The invertible segment is flanked by two sites that are necessary for the inversion and contains a gene (hin) whose product mediates the inversion event. The hin gene shows extensive homology with the TnpR gene carried on the Tn3 transposon. It is also homologous with the gin gene carried on bacteriophage mu. These relationships suggest that the phase variation system may have evolved by the association of a transposon with a resident gene and the subsequent specialization of these elements to regulate flagellar antigen expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simon, M -- Zieg, J -- Silverman, M -- Mandel, G -- Doolittle, R -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1370-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251543" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*genetics ; Base Sequence ; *DNA Transposable Elements ; DNA, Bacterial/genetics ; Flagellin/*genetics ; Genes ; Recombination, Genetic ; Salmonella/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Thyrotropin-releasing hormone precursor: characterization in rat brain (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-10
    Description: To characterize the precursor of mammalian thyrotropin-releasing hormone (TRH), a rat hypothalamic lambda gt11 library was screened with an antiserum directed against a synthetic peptide representing a portion of the rat TRH prohormone. The nucleotide sequence of the immunopositive complementary DNA encoded a protein with a molecular weight of 29,247. This protein contained five copies of the sequence Gln-His-Pro-Gly flanked by paired basic amino acids and could therefore generate five TRH molecules. In addition, potential cleavage sites in the TRH precursor could produce other non-TRH peptides, which may be secreted. In situ hybridization to rat brain sections demonstrated that the pre-proTRH complementary DNA detected neurons concentrated in the parvocellular division of the paraventricular nucleus, the same location as cells detected by immunohistochemistry. These findings indicate that mammalian TRH arises by posttranslational processing of a larger precursor protein. The ability of the TRH prohormone to generate multiple copies of the bioactive peptide may be an important mechanism in the amplification of hormone production.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lechan, R M -- Wu, P -- Jackson, I M -- Wolf, H -- Cooperman, S -- Mandel, G -- Goodman, R H -- AM 34540/AM/NIADDK NIH HHS/ -- CA 37370/CA/NCI NIH HHS/ -- P30 AM 39428/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):159-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3079917" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*physiology ; DNA/genetics ; Hypothalamus/physiology ; Molecular Weight ; Protein Precursors/genetics/*physiology ; Pyrrolidonecarboxylic Acid/analogs & derivatives ; Rats ; Rats, Inbred Strains ; Thyrotropin-Releasing Hormone/genetics/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Genomic organization and deduced amino acid sequence of a putative sodium channel gene in Drosophila (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-08-14
    Description: The deduced amino acid sequence of a Drosophila gene isolated with a vertebrate sodium channel complementary DNA probe revealed an organization virtually identical to the vertebrate sodium channel protein; four homologous domains containing all putative membrane-spanning regions are repeated in tandem with connecting linkers of various sizes. All areas of the protein presumed to be critical for channel function show high evolutionary conservation. These include those proposed to function in voltage-sensitive gating, inactivation, and ion selectivity. All 24 putative gating charges of the vertebrate protein are in identical positions in the Drosophila gene. Ten introns interrupt the coding regions of the four homology units; introns with positions conserved among homology units bracket a region hypothesized to be the selectivity filter for the channel. The Drosophila gene maps to the right arm of the second chromosome in region 60D-E. This position does not coincide with any known mutations that confer behavioral phenotypes, but is close to the seizure locus (60A-B), which has been hypothesized to code for a voltage-sensitive sodium channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Salkoff, L -- Butler, A -- Wei, A -- Scavarda, N -- Giffen, K -- Ifune, C -- Goodman, R -- Mandel, G -- 1 R01 NS24785-01/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1987 Aug 14;237(4816):744-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2441469" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Evolution ; DNA/genetics ; DNA Restriction Enzymes ; Drosophila/*genetics ; Drosophila melanogaster/genetics ; Electrophorus/genetics ; Exons ; Gene Expression Regulation ; Introns ; *Ion Channels ; Membrane Proteins/*genetics ; RNA, Messenger/genetics ; Sequence Homology, Nucleic Acid ; Sodium/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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