RGD Reference Report - Studies of the strand-annealing activity of mammalian hnRNP complex protein A1. - Rat Genome Database

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Studies of the strand-annealing activity of mammalian hnRNP complex protein A1.

Authors: Kumar, A  Wilson, SH 
Citation: Kumar A and Wilson SH, Biochemistry. 1990 Dec 4;29(48):10717-22.
RGD ID: 10045979
Pubmed: PMID:1703006   (View Abstract at PubMed)

A1 is a major core protein of the mammalian hnRNP complex, and as a purified protein of approximately 34 kDa, A1 is a strong single-stranded nucleic acid binding protein. Several lines of evidence suggest that the protein is organized in discrete domains consisting of an N-terminal segment of approximately 22 kDa and a C-terminal segment of approximately 12 kDa. Each of these domains as a purified fragment is capable of binding to both ssDNA and RNA. We report here that A1 and its C-terminal domain fragment are capable of potent strand-annealing activity for base-pair complementary single-stranded polynucleotides of both RNA and DNA. This effect is not stimulated by ATP. Compared with A1 and the C-terminal fragment, the N-terminal domain fragment has negligible annealing activity. These results indicate that A1 has biochemical activity consistent with a strand-annealing role in relevant reactions, such as pre-mRNA splicing.



Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Hnrnpa1RatDNA/DNA annealing activity  IDA  RGD 
Hnrnpa1RatRNA strand annealing activity  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Hnrnpa1  (heterogeneous nuclear ribonucleoprotein A1)


Additional Information