000130536 001__ 130536
000130536 005__ 20190316234442.0
000130536 0247_ $$2doi$$a10.1093/nar/gkm724
000130536 02470 $$2ISI$$a000251336000035
000130536 02470 $$2DAR$$a11687
000130536 037__ $$aARTICLE
000130536 245__ $$aProtein-RNA and protein-protein interactions mediate association of human EST1A/SMG6 with telomerase
000130536 269__ $$a2007
000130536 260__ $$c2007
000130536 336__ $$aJournal Articles
000130536 520__ $$aThe human EST1A/SMG6 polypeptide physically interacts with the chromosome end replication enzyme telomerase. In an attempt to better understand hEST1A function, we have started to dissect the molecular interactions between hEST1A and telomerase. Here, we demonstrate that the interaction between hEST1A and telomerase is mediated by protein-RNA and protein-protein contacts. We identify a domain within hEST1A that binds the telomerase RNA moiety hTR while full-length hEST1A establishes in addition RNase-resistant and hTR-independent protein-protein contacts with the human telomerase reverse transcriptase polypeptide (TERT). Conversely, within hTERT, we identify a hEST1A interaction domain, which comprises hTR-binding activity and RNA-independent hEST1A-binding activity. Purified, recombinant hEST1A binds the telomerase RNA moiety (hTR) with high affinity (apparent overall K(d) = 25 nM) but low specificity. We propose that hEST1A assembles specifically with telomerase in the context of the hTR-hTERT ribonucleoprotein, through the high affinity of hEST1A for hTR and specific protein-protein contacts with hTERT.
000130536 700__ $$aRedon, S.
000130536 700__ $$aReichenbach., P.
000130536 700__ $$0240570$$g168670$$aLingner, J.
000130536 773__ $$j35$$tNucleic Acids Res.$$k20$$q7011-7022
000130536 8564_ $$zURL
000130536 8564_ $$uhttps://infoscience.epfl.ch/record/130536/files/Redon_Nucl-Acids-Research_2008.pdf$$zn/a$$s3950645
000130536 909C0 $$xU11159$$0252147$$pUPLIN
000130536 909CO $$qGLOBAL_SET$$pSV$$ooai:infoscience.tind.io:130536$$particle
000130536 937__ $$aUPLIN-ARTICLE-2008-010
000130536 973__ $$rREVIEWED$$sPUBLISHED$$aEPFL
000130536 980__ $$aARTICLE