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HNRNPA1  -  heterogeneous nuclear ribonucleoprotein A1

Bos taurus

Synonyms: HNRPA1, hnRNP A1
 
 
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Disease relevance of HNRPA1

  • Peptides required to establish the UP1 sequence were isolated by reversed-phase HPLC of digests produced by endoproteinase Lys-C, trypsin, chymotrypsin, Staphylococcus aureus V8 protease, and cyanogen bromide cleavage of UP1 [1].
  • A specific model for the conformation of single-stranded polynucleotides in complex with the helix-destabilizing protein GP32 of bacteriophage T4 [2].
 

High impact information on HNRPA1

  • A complete amino acid sequence has been determined for the UP1 single-stranded DNA binding protein from calf thymus that was first described by G [1].
  • UP1 has a blocked NH2 terminus and contains a single NG,NG-dimethylarginine residue near its COOH terminus [1].
  • The amino acid sequence of UP1 (Williams, K. R., Stone, K. L., LoPresti, M. B., Merrill, B. M., and Planck, S. R. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 5666-5670) reveals that UP1 contains 195 amino acids, including one dimethylarginine residue near its COOH terminus [3].
  • Solid-phase sequencing of three tryptic peptides that together account for 9% of the 39,500-dalton UP2 protein demonstrate that there is a high degree of sequence homology between UP1 and UP2 [3].
  • Utilizing protein tryptophan fluorescence as a probe, polynucleotide binding was shown to stabilize UP1 against thermal unfolding [4].
 

Biological context of HNRPA1

  • In addition to serving as a basis for determining structural relationships among various mammalian single-stranded nucleic acid binding proteins, the amino acid sequence of UP1 reveals that the A1 hnRNP protein contains a region of internal sequence homology that apparently corresponds to two independent nucleic acid binding sites [5].
 

Associations of HNRPA1 with chemical compounds

  • The relative ease with which the UP1 protein was sequenced, requiring only about a year to complete, and the comparatively modest amount of protein required, less than 5 mg, attests to the usefulness of water soluble carbodiimide coupling and solid-phase sequencing for determining the primary structures of proteins [5].
  • Trichloroacetic acid precipitation followed by enzymatic digestion in 2 M urea proved to be the best approach for generating UP1 peptides [5].
  • A comparison of the inhibitory effect of different homopolymers on UP1-induced renaturation of tRNALeu3 does not indicate significant base specificity in UP1 binding, and a 3'-5' ribose phosphate polymer devoid of heterocyclic bases inhibits as well as the homopolynucleotides [6].
 

Analytical, diagnostic and therapeutic context of HNRPA1

  • High pressure liquid chromatography purification of UP1 and UP2, two related single-stranded nucleic acid-binding proteins from calf thymus [3].
  • Circular dichroism measurements on UP1 confirm previous data that this portion of A1 binds single-stranded nucleic acids non-co-operatively [4].

References

  1. Amino acid sequence of the UP1 calf thymus helix-destabilizing protein and its homology to an analogous protein from mouse myeloma. Williams, K.R., Stone, K.L., LoPresti, M.B., Merrill, B.M., Planck, S.R. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  2. A specific model for the conformation of single-stranded polynucleotides in complex with the helix-destabilizing protein GP32 of bacteriophage T4. Scheerhagen, M.A., Bokma, J.T., Vlaanderen, C.A., Blok, J., van Grondelle, R. Biopolymers (1986) [Pubmed]
  3. High pressure liquid chromatography purification of UP1 and UP2, two related single-stranded nucleic acid-binding proteins from calf thymus. Merrill, B.M., LoPresti, M.B., Stone, K.L., Williams, K.R. J. Biol. Chem. (1986) [Pubmed]
  4. Mammalian heterogeneous ribonucleoprotein A1 and its constituent domains. Nucleic acid interaction, structural stability and self-association. Casas-Finet, J.R., Smith, J.D., Kumar, A., Kim, J.G., Wilson, S.H., Karpel, R.L. J. Mol. Biol. (1993) [Pubmed]
  5. Amino acid sequence of UP1, an hnRNP-derived single-stranded nucleic acid binding protein from calf thymus. Merrill, B.M., Lopresti, M.B., Stone, K.L., Williams, K.R. Int. J. Pept. Protein Res. (1987) [Pubmed]
  6. Mechanistic studies of ribonucleic acid renaturation by a helix-destabilizing protein. Karpel, R.L., Miller, N.S., Fresco, J.R. Biochemistry (1982) [Pubmed]
 
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