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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 236 (1993), S. 289-298 
    ISSN: 1617-4623
    Keywords: Caenorhabditis elegans ; Genomic organization ; Na+/H+ antiporter ; Dopa decarboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A previous study of genomic organization described the identification of nine potential coding regions in 150 kb of genomic DNA from the unc-22(IV) region of Caenorhabditis elegans. In this study, we focus on the genomic organization of a small interval of 0.1 map unit bordered on the right by unc-22 and on the left by the left-hand breakpoints of the deficiencies sDf9, sDf19 and sDf65. This small interval at present contains a single mutagenically defined locus, the essential gene let-56. The cosmid C11F2 has previously been used to rescue let-56. Therefore, at least some of C11F2 must reside in the interval. In this paper, we report the characterization of two coding elements that reside on C11F2. Analysis of nucleotide sequence data obtained from cDNAs and cosmid subclones revealed that one of the coding elements closely resembles aromatic amino acid decarboxylases from several species. The other of these coding elements was found to closely resemble a human growth factor activatable Na+/H+ antiporter. Pairs of oligonucleotide primers, predicted from both coding elements, have been used in PCR experiments to position these coding elements between the left breakpoint of sDf19 and the left breakpoint of sDf65, between the essential genes let-653 and let-56.
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  • 2
    ISSN: 1617-4623
    Keywords: Caenorhabditis elegans ; unc-60 ; Muscle ; Actin-binding protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mutations in the unc-60 gene of the nematode Caenorhabditis elegans result in paralysis. The thin filaments of the muscle cells are severely disorganized and not bundled with myosin into functional contractile units. Here we report the cloning and sequence of unc-60. Two unc-60 transcripts, 1.3 and 0.7 kb in size, were detected. The transcripts share a single exon encoding only the initial methionine, yet encode proteins with homologous sequences. The predicted protein products are 165 and 152 amino acids in length and their sequences are 38% identical. Both proteins are homologous to a family of actin depolymerizing proteins identified in vertebrate, plant and protozoan systems. We propose that the unc-60 locus encodes proteins that depolymerize growing actin filaments in muscle cells, and that these proteins are required for the assembly of actin filaments into the contractile myofilament lattice of C. elegans muscle. unc-60 has an essential function in development, since one unc-60 allele, s1586, has a recessive lethal phenotype. Our characterization of s1586 has shown that it is a small deletion which disrupts both coding regions.
    Type of Medium: Electronic Resource
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