Identification and characterisation of a novel human RNA-binding protein.
The processing of heterogeneous nuclear RNA (hnRNA) into a mature message occurs within a number of different nuclear ribonucleoprotein (RNP) complexes which bind to the hnRNA and provide the machinery for these modifying events. Although some components of the nuclear RNP complexes have been isolated, many remain to be elucidated. We report here the isolation of a novel human nucleic-acid-binding protein isolated by screening a lambda gt11 expression library with an oligodeoxyribonucleotide probe. The complete cDNA clone (E5.1) is homologous to a recently published murine sequence. The human gene encodes a ubiquitously expressed mRNA sequence with a putative open reading frame of 305 amino acids and contains a number of domains found in well characterised RNA-binding proteins. The E5.1-derived RNA recognition motif (RRM) is phylogenetically most related to the hnRNP C protein, a component of heterogeneous nuclear RNP particles which participates in mRNA splicing in vitro. E5.1 may, therefore, represent a novel gene, encoding a protein involved in processing of precursor RNAs into mature mRNA.
Bone and Mineral Research Division, Garvan Institute of Medical Research, St. Vincent's Hospital, Sydney, N.S.W., Australia.
J
J
Badolato
E
E
Gardiner
N
N
Morrison
J
J
Eisman
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D016384:Consensus Sequence; D034482:Heterogeneous-Nuclear Ribonucleoprotein Group C; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D006801:Humans; D008969:Molecular Sequence Data; D010802:Phylogeny; D012326:RNA Splicing; D016601:RNA-Binding Proteins / Q000235:genetics*; D012261:Ribonucleoproteins / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D034482:Heterogeneous-Nuclear Ribonucleoprotein Group C; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D016601:RNA-Binding Proteins; C084538:RNPS1 protein, human; D012261:Ribonucleoproteins