PMID- 24703949
OWN - NLM
STAT- MEDLINE
DCOM- 20140723
LR  - 20211021
IS  - 1097-4164 (Electronic)
IS  - 1097-2765 (Print)
IS  - 1097-2765 (Linking)
VI  - 54
IP  - 3
DP  - 2014 May 8
TI  - Structure of a eukaryotic RNase III postcleavage complex reveals a double-ruler 
      mechanism for substrate selection.
PG  - 431-44
LID - S1097-2765(14)00211-1 [pii]
LID - 10.1016/j.molcel.2014.03.006 [doi]
AB  - Ribonuclease III (RNase III) enzymes are a family of double-stranded RNA 
      (dsRNA)-specific endoribonucleases required for RNA maturation and gene 
      regulation. Prokaryotic RNase III enzymes have been well characterized, but how 
      eukaryotic RNase IIIs work is less clear. Here, we describe the structure of the 
      Saccharomyces cerevisiae RNase III (Rnt1p) postcleavage complex and explain why 
      Rnt1p binds to RNA stems capped with an NGNN tetraloop. The structure shows 
      specific interactions between a structural motif located at the end of the Rnt1p 
      dsRNA-binding domain (dsRBD) and the guanine nucleotide in the second position of 
      the loop. Strikingly, structural and biochemical analyses indicate that the dsRBD 
      and N-terminal domains (NTDs) of Rnt1p function as two rulers that measure the 
      distance between the tetraloop and the cleavage site. These findings provide a 
      framework for understanding eukaryotic RNase IIIs.
CI  - Copyright (c) 2014 Elsevier Inc. All rights reserved.
FAU - Liang, Yu-He
AU  - Liang YH
AD  - Biomolecular Structure Section, Macromolecular Crystallography Laboratory, 
      National Cancer Institute, Frederick, MD 21702, USA.
FAU - Lavoie, Mathieu
AU  - Lavoie M
AD  - RNA Group/Groupe ARN, Departement de microbiologie et d'infectiologie, Universite 
      de Sherbrooke, Sherbrooke, Quebec J1E 4K8, Canada.
FAU - Comeau, Marc-Andre
AU  - Comeau MA
AD  - RNA Group/Groupe ARN, Departement de microbiologie et d'infectiologie, Universite 
      de Sherbrooke, Sherbrooke, Quebec J1E 4K8, Canada.
FAU - Abou Elela, Sherif
AU  - Abou Elela S
AD  - RNA Group/Groupe ARN, Departement de microbiologie et d'infectiologie, Universite 
      de Sherbrooke, Sherbrooke, Quebec J1E 4K8, Canada. Electronic address: 
      sherif.abou.elela@usherbrooke.ca.
FAU - Ji, Xinhua
AU  - Ji X
AD  - Biomolecular Structure Section, Macromolecular Crystallography Laboratory, 
      National Cancer Institute, Frederick, MD 21702, USA. Electronic address: 
      jix@mail.nih.gov.
LA  - eng
SI  - PDB/4OOG
GR  - Z99 CA999999/Intramural NIH HHS/United States
GR  - ZIA BC010326-14/Intramural NIH HHS/United States
GR  - CAPMC/CIHR/Canada
PT  - Journal Article
PT  - Research Support, N.I.H., Intramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20140403
PL  - United States
TA  - Mol Cell
JT  - Molecular cell
JID - 9802571
RN  - 0 (RNA, Fungal)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - EC 3.1.26.3 (RNT1 protein, S cerevisiae)
RN  - EC 3.1.26.3 (Ribonuclease III)
SB  - IM
MH  - Amino Acid Sequence
MH  - Catalytic Domain
MH  - Crystallography, X-Ray
MH  - Hydrogen Bonding
MH  - Models, Molecular
MH  - Protein Binding
MH  - RNA Cleavage
MH  - RNA, Fungal/chemistry
MH  - Ribonuclease III/*chemistry
MH  - Saccharomyces cerevisiae/*enzymology
MH  - Saccharomyces cerevisiae Proteins/*chemistry
MH  - Substrate Specificity
PMC - PMC4019767
MID - NIHMS576154
EDAT- 2014/04/08 06:00
MHDA- 2014/07/24 06:00
PMCR- 2015/05/08
CRDT- 2014/04/08 06:00
PHST- 2013/08/14 00:00 [received]
PHST- 2013/12/23 00:00 [revised]
PHST- 2014/02/27 00:00 [accepted]
PHST- 2014/04/08 06:00 [entrez]
PHST- 2014/04/08 06:00 [pubmed]
PHST- 2014/07/24 06:00 [medline]
PHST- 2015/05/08 00:00 [pmc-release]
AID - S1097-2765(14)00211-1 [pii]
AID - 10.1016/j.molcel.2014.03.006 [doi]
PST - ppublish
SO  - Mol Cell. 2014 May 8;54(3):431-44. doi: 10.1016/j.molcel.2014.03.006. Epub 2014 
      Apr 3.