2007
DOI: 10.1107/s1744309106055461
|View full text |Cite
|
Sign up to set email alerts
|

Crystallization and preliminary X-ray analysis ofEscherichia coliRNase HI–dsRNA complexes

Abstract: RNase H binds RNA-DNA hybrid and double-stranded RNA (dsRNA) duplexes with similar affinity, but only cleaves the RNA in the former. To potentially gain insight into the conformational origins of substrate recognition by the enzyme from Escherichia coli, cocrystallization experiments were carried out with RNase HI-dsRNA (enzyme-inhibitor) complexes. Crystals were obtained of two complexes containing 9-mer and 10-mer RNA duplexes that diffracted X-rays to 3.5 and 4 Å resolution, respectively.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

0
7
0

Year Published

2008
2008
2022
2022

Publication Types

Select...
6
1

Relationship

4
3

Authors

Journals

citations
Cited by 7 publications
(7 citation statements)
references
References 45 publications
0
7
0
Order By: Relevance
“…positively charged moieties), hydration, hydrophobic interactions and various stereoelectronic effects. On the other hand, 2′- O -substituted oligonucleotides paired with RNA constitute inhibitors of RNase H [63,64], an endonuclease that is considered a key player in antisense activity due to its ability to degrade the RNA portion of DNA:RNA or PS-DNA:RNA hybrids [11,6570]. This limitation can be overcome to some extent by the use of gap-mer oligonucleotides with central PS-DNA windows and 2′- O -modifications in the flanks [71].…”
Section: 2′-carbohydrate Modificationsmentioning
confidence: 99%
See 1 more Smart Citation
“…positively charged moieties), hydration, hydrophobic interactions and various stereoelectronic effects. On the other hand, 2′- O -substituted oligonucleotides paired with RNA constitute inhibitors of RNase H [63,64], an endonuclease that is considered a key player in antisense activity due to its ability to degrade the RNA portion of DNA:RNA or PS-DNA:RNA hybrids [11,6570]. This limitation can be overcome to some extent by the use of gap-mer oligonucleotides with central PS-DNA windows and 2′- O -modifications in the flanks [71].…”
Section: 2′-carbohydrate Modificationsmentioning
confidence: 99%
“…ref. [70]) and 2′-deoxyriboses opposite RNA at the active site of RNase H were found to prefer a South C2′- endo pucker [69]. Moreover, the enzyme binds DNA and RNA duplexes but is unable to cleave either [66] (a crystal structure of an RNase H:DNA complex has provided insight on the role of double-stranded DNA as an inhibitor [90]).…”
Section: 2′-arabinonucleic Acid Modificationsmentioning
confidence: 99%
“…17, 18) or inhibitor duplexes (dsRNA). 19 Instead, recent crystal structures for the catalytic domains of B. halodurans RNase H ( Bh -RNase HC) 18 and for human RNase H1 ( Hs -RNase HC) 20 in complex with RNA/DNA hybrids have shed light on the conformation of the substrate duplex at the active site of the enzyme. Despite similar affinities for RNA/DNA and dsRNA by RNase H, the geometry of the former duplex clearly deviates from the canonical A-form and the majority of 2′-deoxyriboses adopt puckers more typical of a B-form backbone.…”
Section: Introductionmentioning
confidence: 99%
“…Thus, DF-1 cells were found to be suitable for long-term research. Moreover, with regard to the extent of the enzyme’s activity, RNase HI identifies an RNA–DNA mixture [ 49 , 50 ] and degrades only double-stranded RNA (dsRNA) [ 51 ]. However, RNA–DNA is an intermediate in retrovirus replication.…”
Section: Application Of Ctvi For Different Viral Classesmentioning
confidence: 99%