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Identification of hnRNP A3 as a novel telomere‐binding protein
Author(s) -
Van Wang TzuChien,
Tsai ShengTa,
Huang PeiRong,
Hsieh KaiHsin
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a984-b
Subject(s) - telomere , telomere binding protein , dna , complementary dna , microbiology and biotechnology , biotinylation , biology , dna binding protein , gel electrophoresis , genetics , gene , transcription factor
Telomere is a specialized DNA‐protein structure at the end of linear chromosomes. Human telomeric DNA consists of hundreds to thousands of tandemly repeated hexanucleotides (TTAGGG) and is bound by telomere‐associated proteins to form specialized structure that maintains the integrity of chromosome. In this study, we employed biotinylated‐telomeric DNA to identify novel proteins that interact with the single‐stranded telomeric sequence. The proteins identified by two‐dimensional gel electrophoresis were further characterized by matrix assisted laser desorption ionization time‐of‐flight mass spectrometry (MALDI‐TOF MS) and MALDI‐TOT‐TOF tandem MS. Among the several characterized proteins, we have begun to examine the biochemical and biological functions of a novel protein, hnRNP A3. The cDNA of hnRNP A3 was cloned and expressed in E. coli . The purified hnRNP A3 was shown to bind specifically to telomeric DNA. The domain of hnRNP A3 that confers specific binding to telomeric sequence and the biological role of hnRNP A3 in telomere regulation are presently under investigation.