Ribonuclease E

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Ribonuclease E (EC 3.1.26.12, endoribonuclease E, RNase E, Rne protein) is an enzyme.^[1]^[2]^[3]^[4]^[5]^[6] This enzyme catalyses the following chemical reaction

Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions

RNase E is a bacterial ribonuclease that participates in the processing of ribosomal RNA (9S to 5S rRNA) and the chemical degradation of bulk cellular RNA.

References

↑ Feng, Y., Vickers, T.A. and Cohen, S.N. (2002). "The catalytic domain of RNase E shows inherent 3′ to 5′ directionality in cleavage site selection". Proc. Natl. Acad. Sci. USA 99 (23): 14746–14751. doi:10.1073/pnas.202590899. PMC 137490. PMID 12417756.
↑ Ehretsmann, C.P., Carpousis, A.J. and Krisch, H.M. (1992). "Specificity of Escherichia coli endoribonuclease RNase E: in vivo and in vitro analysis of mutants in a bacteriophage T₄mRNA processing site". Genes Dev. 6 (1): 149–159. doi:10.1101/gad.6.1.149. PMID 1730408.
↑ Cormack, R.S., Genereaux, J.L. and Mackie, G.A. (1993). "RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product". Proc. Natl. Acad. Sci. USA 90 (19): 9006–9010. doi:10.1073/pnas.90.19.9006. PMC 47490. PMID 8415644.
↑ Vanzo, N.F., Li, Y.S., Py, B., Blum, E., Higgins, C.F., Raynal, L.C., Krisch, H.M. and Carpousis, A.J. (1998). "Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome". Genes Dev. 12 (17): 2770–2781. doi:10.1101/gad.12.17.2770. PMC 317140. PMID 9732274.
↑ Steege, D.A. (2000). "Emerging features of mRNA decay in bacteria". RNA 6 (8): 1079–1090. doi:10.1017/S1355838200001023. PMC 1369983. PMID 10943888.
↑ Callaghan, A.J., Grossmann, J.G., Redko, Y.U., Ilag, L.L., Moncrieffe, M.C., Symmons, M.F., Robinson, C.V., McDowall, K.J. and Luisi, B.F. (2003). "Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain". Biochemistry 42 (47): 13848–13855. doi:10.1021/bi0351099. PMID 14636052.

External links

Ribonuclease E at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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