PMID- 17194582
OWN - NLM
STAT- MEDLINE
DCOM- 20070509
LR  - 20240104
IS  - 0959-440X (Print)
IS  - 0959-440X (Linking)
VI  - 17
IP  - 1
DP  - 2007 Feb
TI  - Ribonuclease revisited: structural insights into ribonuclease III family enzymes.
PG  - 138-45
AB  - Ribonuclease III (RNase III) enzymes occur ubiquitously in biology and are 
      responsible for processing RNA precursors into functional RNAs that participate 
      in protein synthesis, RNA interference and a range of other cellular activities. 
      Members of the RNase III enzyme family, including Escherichia coli RNase III, 
      Rnt1, Dicer and Drosha, share the ability to recognize and cleave double-stranded 
      RNA (dsRNA), typically at specific positions or sequences. Recent biochemical and 
      structural data have shed new light on how RNase III enzymes catalyze dsRNA 
      hydrolysis and how substrate specificity is achieved. A major theme emerging from 
      these studies is that accessory domains present in different RNase III enzymes 
      are the key determinants of substrate selectivity, which in turn dictates the 
      specialized biological function of each type of RNase III protein.
FAU - MacRae, Ian J
AU  - MacRae IJ
AD  - Department of Molecular and Cell Biology, Howard Hughes Medical Institute, 
      University of California, Berkeley, CA 94720, USA.
FAU - Doudna, Jennifer A
AU  - Doudna JA
LA  - eng
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Review
DEP - 20061227
PL  - England
TA  - Curr Opin Struct Biol
JT  - Current opinion in structural biology
JID - 9107784
RN  - 0 (Bacterial Proteins)
RN  - 0 (Caenorhabditis elegans Proteins)
RN  - EC 3.1.26.3 (Ribonuclease III)
RN  - EC 3.1.26.3 (drsh-1 protein, C elegans)
SB  - IM
MH  - Bacterial Proteins/chemistry/metabolism
MH  - Caenorhabditis elegans Proteins/chemistry/metabolism
MH  - Models, Molecular
MH  - Protein Conformation
MH  - Ribonuclease III/*chemistry/classification/*metabolism
RF  - 62
EDAT- 2006/12/30 09:00
MHDA- 2007/05/10 09:00
CRDT- 2006/12/30 09:00
PHST- 2006/10/09 00:00 [received]
PHST- 2006/11/09 00:00 [revised]
PHST- 2006/12/13 00:00 [accepted]
PHST- 2006/12/30 09:00 [pubmed]
PHST- 2007/05/10 09:00 [medline]
PHST- 2006/12/30 09:00 [entrez]
AID - S0959-440X(06)00212-0 [pii]
AID - 10.1016/j.sbi.2006.12.002 [doi]
PST - ppublish
SO  - Curr Opin Struct Biol. 2007 Feb;17(1):138-45. doi: 10.1016/j.sbi.2006.12.002. 
      Epub 2006 Dec 27.