hnRNP A2* protein, nucleic acid for coding protein and application thereof

Abstract

The present invention provides an hnRNP A2* protein, nucleic acid for coding the protein and a use thereof. The protein contains a protein, a protein segment or a protein analog or derivative having an amino acid sequence shown as SEQ ID NO.1. The hnRNP A2* protein can actively unloosen telomere G-quadruplexes, bind the minimum binding site at the 3' tail end of telomere, expose five nucleotide tails which can be matched with a telomere enzyme RNA template and promote the extension of telomere under the effect of telomere enzyme, thereby maintaining the cell division potential.

Description

technical field [0001] The invention relates to an hnRNP A2* protein, a nucleic acid encoding the protein and its use, and belongs to the field of biotechnology. Background technique [0002] The ends of human chromosomes are protected by telomeres consisting of TTAGGG repeat DNA sequences and associated proteins. Incomplete end replication of telomeric DNA leaves a 3' single-stranded overhang outside the double-stranded region and causes telomeric DNA to shorten as cells divide. The addition of telomere repeats by telomerase to the 3' end is the main way to compensate for telomere erosion. [0003] In budding yeast, telomere elongation is mediated by Cdc13. Cdc13 is a single-stranded telomeric DNA-binding protein that also binds to the telomerase RNA (Tlc1)-binding protein Est1. Thus, Est2, the catalytic subunit of yeast telomerase, is recruited to telomeres through the following interaction: overhang→Cdc13→Est1→Tlc1→Est2. A similar situation also occurs in Tetrahymena,...

AI Technical Summary

Problems solved by technology

Since POT1 preferentially binds to the minimal binding site (MBS) of 5'-TAGGGTTAG-3' at the 3' end, the binding of POT1 to telomeric DNA leaves a tail less than 5 nucleotides at the 3' end, thereby inhibiting Elongation of linear telomeric substrates, but slightly enhanced elongation of G-quadruplex substrates

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