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The molecular characterization of PRP6 and PRP9 yeast genes reveals a new cysteine/histidine motif common to several splicing factors.
Author(s) -
Legrain P.,
Choulika A.
Publication year - 1990
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1990.tb07465.x
Subject(s) - biology , rna splicing , zinc finger , protein splicing , gene , genetics , peptide sequence , histidine , alternative splicing , rna recognition motif , amino acid , sequence motif , structural motif , biochemistry , rna , exon , transcription factor
prp6 and prp9 thermosensitive (ts) mutants are affected in pre‐mRNA splicing and transport from the nucleus to the cytoplasm. PRP6 and PRP9 wild‐type alleles have been sequenced. DNA sequence analysis reveals homologies in the 5′ and 3′ non‐coding regions, suggesting a common regulation of gene expression. PRP6 and PRP9 genes encode a 899 amino acid and a 530 amino acid protein, respectively. The PRP6 protein has repeated motifs that evoke helix‐loop‐helix structures. Both PRP6 and PRP9 proteins have cysteine/histidine motifs loosely related to those found in zinc finger proteins. The substitution of some, but not all, of these residues by directed mutagenesis has a critical effect on the protein function. Homology searches reveal that two other proteins known to be involved in the nuclear splicing pathway–the yeast PRP11 and the human U1C proteins–contain similar sequences. The five cysteine/histidine motifs found in these four proteins display amino acid similarities in addition to the cysteine and histidine residues, indicating that they participate in biological structures or functions related to the splicing process. In addition, PRP6 and PRP9 exhibit leucine repeat motifs which may be implicated in protein interactions. The prp6 and prp9 ts mutations have been mapped and sequenced.