Human RNase III is a 160-kDa protein involved in preribosomal RNA processing

被引:140
|
作者
Wu, HJ [1 ]
Xu, H [1 ]
Miraglia, LJ [1 ]
Crooke, ST [1 ]
机构
[1] ISIS Pharmaceut, Dept Biol Struct, Carlsbad, CA 92008 USA
关键词
D O I
10.1074/jbc.M005494200
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
A human RNase III gene encodes a protein of 160 kDa with multiple domains, a proline-rich, a serine- and arginine-rich, and an RNase III domain. The expressed purified RNase III domain cleaves double-strand RNA and does not cleave single-strand RNA. The gene is ubiquitously expressed in human tissues and cell lines, and the protein is localized in the nucleus of the cell, The levels of transcription and translation of the protein do not change during different phases of the cell cycle. However, a significant fraction of the protein in the nucleus is translocated to the nucleolus during the S phase of the cell cycle, That this human RNase III is involved in processing of pre-rRNA, but might cleave at sites different from those described for yeast RNase III, is shown by antisense inhibition of RNase III expression. Inhibition of human RNase III expression causes cell death, suggesting an essential role for human RNase III in the cell. The antisense inhibition technique used in this study provides an effective method for functional analysis of newly identified human genes.
引用
收藏
页码:36957 / 36965
页数:9
相关论文
共 50 条
  • [1] Targeted CRISPR disruption reveals a role for RNase MRP RNA in human preribosomal RNA processing
    Goldfarbi, Katherine C.
    Cech, Thomas R.
    GENES & DEVELOPMENT, 2017, 31 (01) : 59 - 71
  • [2] A 160-kDa protein is essential for hemocyanin-derived melanosis of prawn
    Adachi, K
    Hirata, T
    Fujio, A
    Nishioka, T
    Sakaguchi, M
    JOURNAL OF FOOD SCIENCE, 2003, 68 (03) : 765 - 769
  • [3] HEAT SHOCK-INDUCED REDISTRIBUTION OF A 160-KDA NUCLEAR MATRIX PROTEIN
    DEGRAAF, A
    MEIJNE, AML
    VANRENSWOUDE, AJBM
    HUMBEL, BM
    HENEGOUWEN, PMPVE
    DEJONG, L
    VANDRIEL, R
    VERKLEIJ, AJ
    EXPERIMENTAL CELL RESEARCH, 1992, 202 (02) : 243 - 251
  • [4] IDENTIFICATION OF A 160-KDA POLYPEPTIDE THAT BINDS TO THE TIGHT JUNCTION PROTEIN-ZO-1
    GUMBINER, B
    LOWENKOPF, T
    APATIRA, D
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (08) : 3460 - 3464
  • [5] 200-KDA AND 160-KDA NEUROFILAMENT PROTEIN PHOSPHATASE RESISTANCE FOLLOWING IN-VIVO ALUMINUM-CHLORIDE EXPOSURE
    STRONG, MJ
    JAKOWEC, DM
    NEUROTOXICOLOGY, 1994, 15 (04) : 799 - 807
  • [6] RNA PROCESSING BY RNASE-III IS INVOLVED IN THE SYNTHESIS OF ESCHERICHIA-COLI POLYNUCLEOTIDE PHOSPHORYLASE
    TAKATA, R
    MUKAI, T
    HORI, K
    MOLECULAR & GENERAL GENETICS, 1987, 209 (01): : 28 - 32
  • [7] RNase III cleaves eukaryotic preribosomal RNA at a U3 snoRNP-dependent site
    AbouElela, S
    Igel, H
    Ares, M
    CELL, 1996, 85 (01) : 115 - 124
  • [8] ARG-GLY-ASP (RGD) AFFINITY ISOLATION OF A 160-KDA MEMBRANE-PROTEIN FROM LYSATES OF HUMAN-PLATELETS
    LAM, SCT
    PLOW, EF
    FRELINGER, AL
    GINSBERG, MH
    ARTERIOSCLEROSIS, 1988, 8 (05): : A669 - A670
  • [9] Coevolution of RNA and protein subunits in RNase P and RNase MRP, two RNA processing enzymes
    Zhou, Bin
    Wan, Futang
    Lei, Kevin X.
    Lan, Pengfei
    Wu, Jian
    Lei, Ming
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2024, 300 (03)
  • [10] Viral class 1 RNase III involved in suppression of RNA silencing
    Kreuze, JF
    Savenkov, EI
    Cuellar, W
    Li, XD
    Valkonen, JPT
    JOURNAL OF VIROLOGY, 2005, 79 (11) : 7227 - 7238