Xenopus LSm proteins bind U8 snoRNA via an internal evolutionarily conserved octamer sequence

被引:46
作者
Tomasevic, N [1 ]
Peculis, BA [1 ]
机构
[1] NIDDKD, Genet & Biochem Branch, NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1128/MCB.22.12.4101-4112.2002
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
U8 snoRNA plays a unique role in ribosome biogenesis: it is the only snoRNA essential for maturation of the large ribosomal subunit RNAs, 5.8S and 28S. To learn the mechanisms behind the in vivo role of U8 snoRNA, we have purified to near homogeneity and characterized a set of proteins responsible for the formation of a specific U8 RNA-binding complex. This 75-kDa complex is stable in the absence of added RNA and binds U8 with high specificity, requiring the conserved octamer sequence present in all U8 homologues. At least two proteins in this complex can be cross-linked directly to U8 RNA. We have identified the proteins as Xenopus homologues of the LSm (like Sm) proteins, which were previously reported to be involved in cytoplasmic degradation of mRNA and nuclear stabilization of U6 snRNA. We have identified LSm2, -3, -4, -6, -7, and -8 in our purified complex and found that this complex associates with U8 RNA in vivo. This purified complex can bind U6 snRNA in vitro but does not bind U3 or U14 snoRNA in vitro, demonstrating that the LSm complex specifically recognizes U8 RNA.
引用
收藏
页码:4101 / 4112
页数:12
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共 61 条
[1]   A doughnut-shaped heteromer of human Sm-like proteins binds to the 3′-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro [J].
Achsel, T ;
Brahms, H ;
Kastner, B ;
Bachi, A ;
Wilm, M ;
Lührmann, R .
EMBO JOURNAL, 1999, 18 (20) :5789-5802
[2]   The Sm domain is an ancient RNA-binding motif with oligo(U) specificity [J].
Achsel, T ;
Stark, H ;
Lührmann, R .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (07) :3685-3689
[3]   ANTISENSE SNORNAS - A FAMILY OF NUCLEOLAR RNAS WITH LONG COMPLEMENTARITIES TO RIBOSOMAL-RNA [J].
BACHELLERIE, JP ;
MICHOT, B ;
NICOLOSO, M ;
BALAKIN, A ;
NI, JW ;
FOURNIER, MJ .
TRENDS IN BIOCHEMICAL SCIENCES, 1995, 20 (07) :261-264
[4]   Guiding ribose methylation of rRNA [J].
Bachellerie, JP ;
Cavaille, J .
TRENDS IN BIOCHEMICAL SCIENCES, 1997, 22 (07) :257-261
[5]   The NIEHS Xenopus maternal EST project:: interim analysis of the first 13,879 ESTs from unfertilized eggs [J].
Blackshear, PJ ;
Lai, WS ;
Thorn, JM ;
Kennington, EA ;
Staffa, NG ;
Moore, DT ;
Bouffard, GG ;
Beckstrom-Sternberg, SM ;
Touchman, JW ;
Bonaldo, MD ;
Soares, MB .
GENE, 2001, 267 (01) :71-87
[6]   A small nucleolar RNP protein is required for pseudouridylation of eukaryotic ribosomal RNAs [J].
BousquetAntonelli, C ;
Henry, Y ;
Gelugne, JP ;
CaizerguesFerrer, M ;
Kiss, T .
EMBO JOURNAL, 1997, 16 (15) :4770-4776
[7]   A Sm-like protein complex that participates in mRNA degradation [J].
Bouveret, E ;
Rigaut, G ;
Shevchenko, A ;
Wilm, M ;
Séraphin, B .
EMBO JOURNAL, 2000, 19 (07) :1661-1671
[8]   The yeast nucleolar protein Cbf5p is involved in rRNA biosynthesis and interacts genetically with the RNA polymerase I transcription factor RRN3 [J].
Cadwell, C ;
Yoon, HJ ;
Zebarjadian, Y ;
Carbon, J .
MOLECULAR AND CELLULAR BIOLOGY, 1997, 17 (10) :6175-6183
[9]   Crystal structure of a heptameric Sm-like protein complex from archaea: Implications for the structure and evolution of snRNPs [J].
Collins, BM ;
Harrop, SJ ;
Kornfeld, GD ;
Dawes, IW ;
Curmi, PMG ;
Mabbutt, BC .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 309 (04) :915-923
[10]   Role of the ITS2-proximal stem and evidence for indirect recognition of processing sites in pre-rRNA processing in yeast [J].
Côté, CA ;
Peculis, BA .
NUCLEIC ACIDS RESEARCH, 2001, 29 (10) :2106-2116