PMID- 19161841
OWN - NLM
STAT- MEDLINE
DCOM- 20090302
LR  - 20090123
IS  - 1557-7988 (Electronic)
IS  - 0076-6879 (Linking)
VI  - 447
DP  - 2008
TI  - New approaches to understanding double-stranded RNA processing by ribonuclease 
      III purification and assays of homodimeric and heterodimeric forms of RNase III 
      from bacterial extremophiles and mesophiles.
PG  - 119-29
LID - 10.1016/S0076-6879(08)02207-6 [doi]
AB  - Ribonuclease III (RNase III) is a double-stranded (ds)-RNA-specific endonuclease 
      that plays essential roles in the maturation and decay of coding and noncoding 
      RNAs. Bacterial RNases III are structurally the simplest members of the RNase III 
      family, which includes the eukaryotic orthologs Dicer and Drosha. High-resolution 
      crystal structures of RNase III of the hyperthermophilic bacteria Aquifex 
      aeolicus and Thermotoga maritima are available. A. aeolicus RNase III also has 
      been cocrystallized with dsRNA or specific hairpin substrates. These structures 
      have provided essential structural insight to the mechanism of dsRNA recognition 
      and cleavage. However, comparatively little is known about the catalytic 
      behaviors of A. aeolicus or T. maritima RNases III. This chapter provides 
      protocols for the purification of A. aeolicus and T. maritima RNases III and also 
      describes the preparation of artificial heterodimers of Escherichia coli RNase 
      III, which are providing new insight on the subunit and domain interactions 
      involved in dsRNA recognition and cleavage.
FAU - Meng, Wenzhao
AU  - Meng W
AD  - Department of Chemistry, Temple University, Philadelphia, Pennsylvania, USA.
FAU - Nicholson, Rhonda H
AU  - Nicholson RH
FAU - Nathania, Lilian
AU  - Nathania L
FAU - Pertzev, Alexandre V
AU  - Pertzev AV
FAU - Nicholson, Allen W
AU  - Nicholson AW
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Methods Enzymol
JT  - Methods in enzymology
JID - 0212271
RN  - 0 (RNA, Double-Stranded)
RN  - EC 3.1.26.3 (Ribonuclease III)
SB  - IM
MH  - Base Sequence
MH  - Chromatography, Affinity
MH  - Dimerization
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Escherichia coli/*enzymology
MH  - Inclusion Bodies/enzymology
MH  - RNA, Double-Stranded/chemistry/metabolism
MH  - Ribonuclease III/chemistry/isolation & purification/*metabolism
MH  - Substrate Specificity
MH  - Thermotoga maritima/*enzymology
EDAT- 2009/01/24 09:00
MHDA- 2009/03/03 09:00
CRDT- 2009/01/24 09:00
PHST- 2009/01/24 09:00 [entrez]
PHST- 2009/01/24 09:00 [pubmed]
PHST- 2009/03/03 09:00 [medline]
AID - S0076-6879(08)02207-6 [pii]
AID - 10.1016/S0076-6879(08)02207-6 [doi]
PST - ppublish
SO  - Methods Enzymol. 2008;447:119-29. doi: 10.1016/S0076-6879(08)02207-6.