Abstract
The specificity of RNase III for various synthetic homopolymeric doublestranded RNA substrates have been examined. Although RNase III appears to cleave all homopolymeric RNA duplex structures, with Poly (U)·Poly (A) as the substrate, the enzyme cleaves the Poly (U) strand much faster than it cleaves the Poly (A) strand. Under conditions where the Poly (U) strand is quantitatively cleaved into acid-soluble fragments ranging in size between 5-8 nucleotides in length, the poly (A) strand is cleaved into large fragments 40-60 nucleotides in length. These results indicate that RNase III recognizes duplex RNA structures for binding, and makes single-stranded scissions and suggests that the enzyme has a preference for cleaving adjacent to UMP residues over AMP residues in polynucleotide chains.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 306-313 |
| Number of pages | 8 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 73 |
| Issue number | 2 |
| DOIs | |
| State | Published - Nov 22 1976 |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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Specificity of cleavage by ribonuclease III. / Bishayee, Subal; Maitra, Umadas.
In: Biochemical and Biophysical Research Communications, Vol. 73, No. 2, 22.11.1976, p. 306-313.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Specificity of cleavage by ribonuclease III
AU - Bishayee, Subal
AU - Maitra, Umadas
PY - 1976/11/22
Y1 - 1976/11/22
N2 - The specificity of RNase III for various synthetic homopolymeric doublestranded RNA substrates have been examined. Although RNase III appears to cleave all homopolymeric RNA duplex structures, with Poly (U)·Poly (A) as the substrate, the enzyme cleaves the Poly (U) strand much faster than it cleaves the Poly (A) strand. Under conditions where the Poly (U) strand is quantitatively cleaved into acid-soluble fragments ranging in size between 5-8 nucleotides in length, the poly (A) strand is cleaved into large fragments 40-60 nucleotides in length. These results indicate that RNase III recognizes duplex RNA structures for binding, and makes single-stranded scissions and suggests that the enzyme has a preference for cleaving adjacent to UMP residues over AMP residues in polynucleotide chains.
AB - The specificity of RNase III for various synthetic homopolymeric doublestranded RNA substrates have been examined. Although RNase III appears to cleave all homopolymeric RNA duplex structures, with Poly (U)·Poly (A) as the substrate, the enzyme cleaves the Poly (U) strand much faster than it cleaves the Poly (A) strand. Under conditions where the Poly (U) strand is quantitatively cleaved into acid-soluble fragments ranging in size between 5-8 nucleotides in length, the poly (A) strand is cleaved into large fragments 40-60 nucleotides in length. These results indicate that RNase III recognizes duplex RNA structures for binding, and makes single-stranded scissions and suggests that the enzyme has a preference for cleaving adjacent to UMP residues over AMP residues in polynucleotide chains.
UR - http://www.scopus.com/inward/record.url?scp=0017109665&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0017109665&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(76)90708-7
DO - 10.1016/0006-291X(76)90708-7
M3 - Article
C2 - 999712
AN - SCOPUS:0017109665
VL - 73
SP - 306
EP - 313
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -