Abstract
RNase R and RNase II are the two representatives from the RNR family of processive, 3' to 5' exoribonucleases in Esche richia coli. Although RNase II is specific for single-stranded RNA, RNase R readily degrades through structured RNA. Furthermore, RNase R appears to be the only known 3' to 5' exoribonuclease that is able to degrade through double-stranded RNA without the aid of a helicase activity. Consequently, its functional domains and mechanism of action are of great interest. Using a series of truncated RNase R proteins we show that the cold-shock and S1 domains contribute to substrate binding. The cold-shock domains appear to play a role in substrate recruitment, whereas the S1 domain is most likely required to position substrates for efficient catalysis. Most importantly, the nuclease domain alone, devoid of the cold-shock and S1 domains, is sufficient for RNase R to bind and degrade structured RNAs. Moreover, this is a unique property of the nuclease domain of RNase R because this domain in RNase II stalls as it approaches a duplex. We also show that the nuclease domain of RNase R binds RNA more tightly than the nuclease domain of RNase II. This tighter binding may help to explain the difference in catalytic properties between RNase R and RNase II.
| Original language | English |
|---|---|
| Pages (from-to) | 486-494 |
| Number of pages | 9 |
| Journal | Journal of Biological Chemistry |
| Volume | 284 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 2 2009 |
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ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Molecular Biology
Cite this
The roles of individual domains of R Nase R in substrate binding and exoribonuclease activity the nuclease domain is sufficient for digestion of structured RNA. / Vincent, Helen A.; Deutscher, Murray P.
In: Journal of Biological Chemistry, Vol. 284, No. 1, 02.01.2009, p. 486-494.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The roles of individual domains of R Nase R in substrate binding and exoribonuclease activity the nuclease domain is sufficient for digestion of structured RNA
AU - Vincent, Helen A.
AU - Deutscher, Murray P
PY - 2009/1/2
Y1 - 2009/1/2
N2 - RNase R and RNase II are the two representatives from the RNR family of processive, 3' to 5' exoribonucleases in Esche richia coli. Although RNase II is specific for single-stranded RNA, RNase R readily degrades through structured RNA. Furthermore, RNase R appears to be the only known 3' to 5' exoribonuclease that is able to degrade through double-stranded RNA without the aid of a helicase activity. Consequently, its functional domains and mechanism of action are of great interest. Using a series of truncated RNase R proteins we show that the cold-shock and S1 domains contribute to substrate binding. The cold-shock domains appear to play a role in substrate recruitment, whereas the S1 domain is most likely required to position substrates for efficient catalysis. Most importantly, the nuclease domain alone, devoid of the cold-shock and S1 domains, is sufficient for RNase R to bind and degrade structured RNAs. Moreover, this is a unique property of the nuclease domain of RNase R because this domain in RNase II stalls as it approaches a duplex. We also show that the nuclease domain of RNase R binds RNA more tightly than the nuclease domain of RNase II. This tighter binding may help to explain the difference in catalytic properties between RNase R and RNase II.
AB - RNase R and RNase II are the two representatives from the RNR family of processive, 3' to 5' exoribonucleases in Esche richia coli. Although RNase II is specific for single-stranded RNA, RNase R readily degrades through structured RNA. Furthermore, RNase R appears to be the only known 3' to 5' exoribonuclease that is able to degrade through double-stranded RNA without the aid of a helicase activity. Consequently, its functional domains and mechanism of action are of great interest. Using a series of truncated RNase R proteins we show that the cold-shock and S1 domains contribute to substrate binding. The cold-shock domains appear to play a role in substrate recruitment, whereas the S1 domain is most likely required to position substrates for efficient catalysis. Most importantly, the nuclease domain alone, devoid of the cold-shock and S1 domains, is sufficient for RNase R to bind and degrade structured RNAs. Moreover, this is a unique property of the nuclease domain of RNase R because this domain in RNase II stalls as it approaches a duplex. We also show that the nuclease domain of RNase R binds RNA more tightly than the nuclease domain of RNase II. This tighter binding may help to explain the difference in catalytic properties between RNase R and RNase II.
UR - http://www.scopus.com/inward/record.url?scp=58649092877&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=58649092877&partnerID=8YFLogxK
U2 - 10.1074/jbc.M806468200
DO - 10.1074/jbc.M806468200
M3 - Article
C2 - 19004832
AN - SCOPUS:58649092877
VL - 284
SP - 486
EP - 494
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 1
ER -