Pof8 is a La-related protein and a constitutive component of telomerase in fission yeast

被引:24
|
作者
Paez-Moscoso, Diego J. [1 ]
Pan, Lili [1 ]
Sigauke, Rutendo F. [1 ]
Schroeder, Morgan R. [1 ]
Tang, Wen [1 ,5 ]
Baumann, Peter [1 ,2 ,3 ,4 ]
机构
[1] Stowers Inst Med Res, Kansas City, MO 64110 USA
[2] Howard Hughes Med Inst, Kansas City, MO 64110 USA
[3] Univ Kansas, Med Ctr, Dept Mol & Integrat Physiol, Kansas City, KS 66160 USA
[4] Johannes Gutenberg Univ Mainz, Inst Dev Biol & Neurobiol, D-55099 Mainz, Germany
[5] Univ Massachusetts, Med Sch, RNA Therapeut Inst, Worcester, MA 01605 USA
来源
NATURE COMMUNICATIONS | 2018年 / 9卷
关键词
NUCLEAR RIBONUCLEOPROTEIN PARTICLE; SCHIZOSACCHAROMYCES-POMBE; 3' END; RNA; LENGTH; HOLOENZYME; SUBUNIT; P65; P43; IDENTIFICATION;
D O I
10.1038/s41467-017-02284-8
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Telomerase reverse transcriptase (TERT) and the non-coding telomerase RNA subunit (TR) constitute the core of telomerase. Here we now report that the putative F-box protein Pof8 is also a constitutive component of active telomerase in fission yeast. Pof8 functions in a hierarchical assembly pathway by promoting the binding of the Lsm2-8 complex to telomerase RNA, which in turn promotes binding of the catalytic subunit. Loss of Pof8 reduces TER1 stability, causes a severe assembly defect, and results in critically short telomeres. Structure profile searches identified similarities between Pof8 and telomerase subunits from ciliated protozoa, making Pof8 next to TERT the most widely conserved telomerase subunits identified to date.
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页数:11
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