RNP-T, a ribonucleoprotein from Arabidopsis thaliana, contains two RNP-80 motifs and a novel acidic repeat arranged in an alpha-helix conformation.
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 lambda gt11 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 alpha-helix conformation. We propose that the acidic patch might play a role in protein-protein interaction.
Bar-Zvi
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Department of Life Sciences, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Shagan
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T
Schindler
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Cashmore
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AR
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics*; D029681:Arabidopsis Proteins; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D017433:Protein Structure, Secondary; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000235:genetics*; D012091:Repetitive Sequences, Nucleic Acid; D012261:Ribonucleoproteins / Q000737:chemistry / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
D029681:Arabidopsis Proteins; D015345:Oligonucleotide Probes; D016601:RNA-Binding Proteins; C078704:RNP-T protein, Arabidopsis; D012261:Ribonucleoproteins; D004247:DNA