The yeast homolog of human PinX1 is involved in rRNA and small nucleolar RNA maturation, not in telomere elongation inhibition

被引:71
作者
Guglielmi, B [1 ]
Werner, M [1 ]
机构
[1] CEA Saclay, Serv Biochim & Genet Mol, F-91191 Gif Sur Yvette, France
关键词
D O I
10.1074/jbc.M205526200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In human cells, PinX1 protein has recently been shown to regulate telomere length by repressing the telomerase. In this work, we show that the putative yeast homolog of PinX1, encoded by the YGR280c open reading frame (ORF), is a new component of the ribosomal RNA processing machinery. The protein has a KK(E/D) C-terminal domain typical of nucleolar proteins and bears a putative RNA interacting domain widespread in eukaryotes called the G-patch. The protein was hence renamed Gno1p (G-patch nucleolar protein). GNO1 deletion results in a large growth defect due to the inhibition of the pre-ribosomal RNA processing first cleavage steps at sites A(0), A(1), and A(2). Furthermore, Gno1p is involved in the final 3'-end trimming of U18 and U24 small nucleolar RNAs. A mutational analysis showed that the G-patch of Gno1p is essential for both functions, whereas the KK(E/D) repeats are only required for U18 small nucleolar RNA maturation. We found that PinX1 complemented the gno1-Delta mutation, suggesting that it has a dual function in telomere length regulation and ribosomal RNA maturation in agreement with its telomeric and nucleolar localization in human cells. Conversely, we found that Gno1p does not exhibit the in vivo telomerase inhibitor activity of PinX1.
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页码:35712 / 35719
页数:8
相关论文
共 42 条
[1]   The yeast exosome and human PM-Scl are related complexes of 3′→5′ exonucleases [J].
Allmang, C ;
Petfalski, E ;
Podtelejnikov, A ;
Mann, M ;
Tollervey, D ;
Mitchell, P .
GENES & DEVELOPMENT, 1999, 13 (16) :2148-2158
[2]   Functions of the exosome in rRNA, snoRNA and snRNA synthesis [J].
Allmang, C ;
Kufel, J ;
Chanfreau, G ;
Mitchell, P ;
Petfalski, E ;
Tollervey, D .
EMBO JOURNAL, 1999, 18 (19) :5399-5410
[3]   Degradation of ribosomal RNA precursors by the exosome [J].
Allmang, Christine ;
Mitchell, Philip ;
Petfalski, Elisabeth ;
Tollervey, David .
NUCLEIC ACIDS RESEARCH, 2000, 28 (08) :1684-1691
[4]   G-patch: a new conserved domain in eukaryotic RNA-processing proteins and type D retroviral polyproteins [J].
Aravind, L ;
Koonin, EV .
TRENDS IN BIOCHEMICAL SCIENCES, 1999, 24 (09) :342-344
[5]   The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution [J].
Ban, N ;
Nissen, P ;
Hansen, J ;
Moore, PB ;
Steitz, TA .
SCIENCE, 2000, 289 (5481) :905-920
[6]   Cross Talk between tRNA and rRNA synthesis in Saccharomyces cerevisiae [J].
Briand, JF ;
Navarro, F ;
Gadal, O ;
Thuriaux, P .
MOLECULAR AND CELLULAR BIOLOGY, 2001, 21 (01) :189-195
[7]  
CARLES C, 1998, TRANSCRIPTION RIBOSO, V1, P9
[8]   Remodeling of yeast genome expression in response to environmental changes [J].
Causton, HC ;
Ren, B ;
Koh, SS ;
Harbison, CT ;
Kanin, E ;
Jennings, EG ;
Lee, TI ;
True, HL ;
Lander, ES ;
Young, RA .
MOLECULAR BIOLOGY OF THE CELL, 2001, 12 (02) :323-337
[9]   Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3′ end formation of 5.8S rRNA in Saccharomyces cerevisiae [J].
de la Cruz, J ;
Kressler, D ;
Tollervey, D ;
Linder, P .
EMBO JOURNAL, 1998, 17 (04) :1128-1140
[10]  
Delage Yves, 1903, HEREDITE GRANDS PROB