Abstract:
:Telomerase is an almost universal cancer target that consists minimally of a core protein human telomerase reverse transcriptase (hTERT) and a RNA component human telomerase RNA (hTR). Some inhibitors of this enzyme are thought to function by the covalent binding to one or several cysteine residues; however, this inhibition mechanism has never been investigated because of the difficulty in producing telomerase. In this study, we use a recent method to produce recombinant hTERT to analyze the effect of cysteine-reactive inhibitors on telomerase. Using mass spectrometry and mutagenesis analysis, we identify several targeted residues in separated domains of the hTERT protein and show that cysteine-reactive reagents abolish the interaction with the CR4/5 region of hTR.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kellermann G,Dingli F,Masson V,Dauzonne D,Ségal-Bendirdjian E,Teulade-Fichou MP,Loew D,Bombard Sdoi
10.1002/1873-3468.12589subject
Has Abstractpub_date
2017-03-01 00:00:00pages
863-874issue
6eissn
0014-5793issn
1873-3468journal_volume
591pub_type
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