Dataset Information

Identification of telomere-binding proteins by enChIP-MS

ABSTRACT: We identified the telomere associated molecules by engineered DNA-binding molecule-mediated chromatin immunoprecipitaion (enChIP). Purified proteins were analyzed by GeLC-MS/MS. Tandem mass spectra were extracted by Proteome Discoverer 1.2. Database searchs were submitted to an in-house Mascot server version 2.4.1. Mascot was set up to search the Swissprot database assuming the digestion enzyme as trypsin. Carbamidomethylation of cysteine was set as a fixed modification. Oxidized methionine, acetylation of N terminus and conversion of glutamine to Pyro-Glu at N terminus were set as variable modifications. The precursor mass tolerances were 10 ppm and the tolerance of the MS/MS ions was 0.8 Da. In Scaffold 3.4.5, database search results were grouped according to gel bands.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Ba/f3 Cell

SUBMITTER: Kazunobu Saito

LAB HEAD: Kazunobu Saito

PROVIDER: PXD000461 | Pride | 2013-11-12

REPOSITORIES: Pride

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Identification of telomere-associated molecules by engineered DNA-binding molecule-mediated chromatin immunoprecipitation (enChIP).

Fujita Toshitsugu T Asano Yoshinori Y Ohtsuka Junko J Takada Yoko Y Saito Kazunobu K Ohki Rieko R Fujii Hodaka H

Scientific reports 20131108

Biochemical analysis of molecular interactions in specific genomic regions requires their isolation while retaining molecular interactions in vivo. Here, we report isolation of telomeres by engineered DNA-binding molecule-mediated chromatin immunoprecipitation (enChIP) using a transcription activator-like (TAL) protein recognizing telomere repeats. Telomeres recognized by the tagged TAL protein were immunoprecipitated with an antibody against the tag and subjected to identification of telomere-b ...[more]

PMID: 24201379

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