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  • sequence  (2)
  • Springer  (2)
  • 1990-1994  (1)
  • 1985-1989  (1)
  • 1
    Electronic Resource
    Electronic Resource
    RNP-T, a ribonucleoprotein from Arabidopsis thaliana, contains two RNP-80 motifs and a novel acidic repeat arranged in an α-helix conformation (1992)
    Springer
    Plant molecular biology 20 (1992), S. 833-838 
    Details
    ISSN: 1573-5028
    Keywords: Arabidopsis ; cloning ; ribonucleoprotein ; RNA-binding ; RNP ; sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have isolated a 1148 bp long cDNA clone encoding an RNA-binding protein in Arabidopsis. Several partial cDNA clones were isolated by screening an Arabidopsis λgt11 expression library for the binding of DNA. One of these clones was used as a probe to isolate a full-length clone. The 329 amino acid protein, termed RNP-T, contains in its carboxy terminus two adjacent RNP-80 motifs, a previously described 80 amino acid long conserved putative RNA-binding domain. Each RNP-80 motif includes both consensus short sequences, RNP1 and RNP2, which are separated by 33 amino acids. We have identified an acidic domain of 54 amino acids, which is located amino-terminal to the RNP-80 motifs. Seven tandem repeats of a hexamer are present within this domain. This acidic domain has a potential α-helix conformation. We propose that the acidic patch might play a role in protein-protein interaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00027154
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  • 2
    Electronic Resource
    Electronic Resource
    Four genes in two diverged subfamilies encode the ribulose-1,5-bisphosphate carboxylase small subunit polypeptides of Arabidopsis thaliana (1988)
    Springer
    Plant molecular biology 11 (1988), S. 745-759 
    Details
    ISSN: 1573-5028
    Keywords: Arabidopsis thaliana ; multigene family ; ribulose-1,5-bisphosphate carboxylase ; sequence ; small subunit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The multigene family encoding the small subunit polypeptides of ribulose-1,5-bisphosphate carboxylase/oxygenase in the crucifer Arabidopsis thaliana has been isolated and the organization and structure of the individual members determined. The family consists of four genes which have been divided into two subfamilies on the basis of linkage and DNA and amino acid sequence similarities. Three of the genes, designated ats1B, ats2B, and ats3B, reside in tandem on an 8 kb stretch of the chromosome. These genes share greater than 95% similarity in DNA sequence and encode polypeptides identical in length and 96.7% similar in amino acid sequence. The fourth gene, ats1A, is at least 10 kb removed from, or completely unlinked to the B subfamily. The B subfamily genes are more similar to each other than to ats1A in nucleotide and amino acid sequence. All four genes are interupted by two introns whose placement within the coding region of the genes is conserved. The introns of the B subfamily genes are similar in length and nucleotide sequence, but show no similarity to the introns of ats1A. Comparison of the DNA sequences within the immediate 5′ and 3′ flanking sequences among the genes revealed only limited regions of homology. S1 analysis shows that all four genes are expressed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00019515
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