Recombinant expression and domain structure of the Rna1 protein from Schizosaccharomyces pombe.
The amino acid sequence of Rna1p, a yeast protein implicated in the maturation and/or nucleocytoplasmic transport of RNA, is characterised by the presence of eight leucine-rich repeats (LLRs) as well as two intervening repeats of a different type and a highly acidic C-terminal region. Limited proteolysis of purified Rna1p expressed recombinantly in bacteria reveals that the C-terminal extension but not the region containing the two types of repeats is highly accessible to proteolytic attack and that the C-terminal region most likely harbours (a) low affinity Ca(2+)-binding site(s). These results are indicative of the domain structure of the Rna1p molecule, with the repeats and the C-terminal region being accessible for different interactions.
Haberland
J
J
Max Planck Institute for Biophysical Chemistry, Department of Biochemistry, Göttingen, Germany.
Gerke
V
V
D001483:Base Sequence; D003001:Cloning, Molecular; D010450:Endopeptidases / Q000378:metabolism; D004926:Escherichia coli; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D020690:GTPase-Activating Proteins; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D012568:Schizosaccharomyces / Q000235:genetics* / Q000378:metabolism; D029702:Schizosaccharomyces pombe Proteins
D005656:Fungal Proteins; D020690:GTPase-Activating Proteins; D011994:Recombinant Proteins; D029702:Schizosaccharomyces pombe Proteins; C499298:rna1 protein, S pombe; D010450:Endopeptidases