Temp

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Ribonuclease (RNase) degrades RNA. The endonucleases cleave single or double stranded RNA and include RNase III, A, T1 H and P. Exo-RNases remove terminal nucleotide from the ends of the RNA molecule. They include RNase II D, T, PH, Polynucleotide Phosphorylase (PNPase) and oligoribonuclease (ORNase).


  • RNase A cleaves C or U of single-stranded RNA (ssRNA).
  • RNase BA is RNase from Bacillus amyloliquefaciens.
  • RNase D degrades 3'-end pre-tRNA.
  • RNase H cleaves RNA/DNA double-strand to produce ssDNA.
  • RNase I cleaves 3'-end of ssRNA.
  • RNase II degrades 3'-end ssRNA.
  • RNase III cleaves rRNA.
  • RNase 5 is known as angiogenin and is a potent stimulator of new blood vessels formation.
  • RNase P is a ribozyme.
  • RNase S is RNase A cleaved by subtilisin.
  • RNase SA is RNase from Streptomyces auerofaciens.
  • RNase T is involved in RNA maturation.
  • RNase T1 cleaves 3'-end G from ssRNA.
  • RNase U2 cleaves 3'-end A from ssRNA.
  • α-sarcin is a cytotoxic RNase which cleaves a phosphodiester bond in a conserved rRNA loop and inactivates the ribosome.
  • oligoribonuclease is an exoribonuclease which cleaves 3'-end of viral RNA-DNA hybrid.
  • Polynucleotide phosphorylase is a bifunctional enzyme which has exoribonuclease activity.
  • Binase is a microbial RNase which cleaves endonucleolyticly ssRNA.
  • Poly(A)-specific RNase cleaves exonucleolyticly the poly(A) tail.

For more details on RNase A see:


For RNase B and RNase S see RNaseS RNaseB.

Active Site of Ribonuclease A

Ribonuclease A cleaves RNA strands by catalyzing a transphosphorylation reaction where the 2'-OH of the ribose sugar attacks the neighboring phosphate, releasing the ribose on the the other side of the phosphate. This structure shows ribonuclease A (in blue) bound to short DNA strand composed of four thymidines (in pink). Ribonuclease binds tightly to DNA, but since DNA is missing the 2'-OH, ribonuclease does not cleave it. are shown that are important for catalysis. The 3' carbon on the DNA is shown in red--it is the site where the 2'-OH is connected in RNA. The two histidines perform the proton transfers that are needed in the reaction, and the lysine stabilizes the intermediate that is formed as the 2'-OH attacks the phosphate. Ribonuclease cleaves RNA strands best next to cytidine and uridine nucleotides--the reason for this may be seen in a . Notice that the small pyrimidine base is surrounded by protein atoms. A larger purine base would not fit well in this space.[1]

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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=>

This is a default text for your page Temp. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [2] or to the article describing Jmol [3] to the rescue.

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Disease

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Structural highlights

PDB ID 1rta

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3D structures of ribonuclease3D structures of ribonuclease

Updated on 21-December-2014


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ReferencesReferences

  1. ↑ Birdsall DL, McPherson A. Crystal structure disposition of thymidylic acid tetramer in complex with ribonuclease A. J Biol Chem. 1992 Nov 5;267(31):22230-6. PMID:1429575
  2. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  3. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

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Michal Harel
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