Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.26.12 extracted from

  • Nishio, S.Y.; Itoh, T.
    Arginine-rich RNA binding domain and protein scaffold domain of RNase E are important for degradation of RNAI but not for that of the Rep mRNA of the ColE2 plasmid (2009), Plasmid, 62, 83-87.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information RNase E cleaves the 217-nt RNAs at internal sites in an arginine-rich RNA binding domain-independent manner and about 180-nt degradation intermediates are formed Escherichia coli ?
-
?
Rep mRNA + H2O the arginine-rich RNA binding domain and the protein scaffold domain of RNase E are dispensable for degradation of the replication initiator protein (Rep) mRNA of the ColE2 plasmid Escherichia coli ?
-
?
RNA I + H2O the arginine-rich RNA binding domain of RNase E and the protein scaffold domain of RNase E is important for successive exoribonucleolytic degradation of RNAI, suggesting involvement of RhlB. RNase E-PNPase complex formation is not essential for RNAI degradation Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
RNase E
-
Escherichia coli

General Information

General Information Comment Organism
malfunction RNAI signals of the DELTA225 mutant lacking the PNPase binding region are similar to those of the wild-type strain. RNAI degradation intermediate accumulates in the DELTA374 mutant lacking the PNPase binding region and protein scaffold domain, which binds to RhlB and enolase, as compared with that in the wild-type strain Escherichia coli