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

BRENDA support

Literature summary for 3.6.4.13 extracted from

  • Ranji, A.; Shkriabai, N.; Kvaratskhelia, M.; Musier-Forsyth, K.; Boris-Lawrie, K.
    Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognition and translation of complex mRNAs (2011), J. Biol. Chem., 286, 5328-5337.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.13

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL-21 Homo sapiens

Protein Variants

Protein Variants Comment Organism
K236E mutant exhibits relatively minor reduction in interaction with SNV PCE Homo sapiens
K54A/K55A mutant exhibits relatively minor reduction in interaction with SNV PCE Homo sapiens
K54A/K55A/K236E triple mutant shows a severe reduction in interaction with junD post-transcriptional control element (PCE) or SNV PCE compared with wild-type Homo sapiens
additional information recombinant RHA domains are evaluated for binding activity to post-transcriptional control element (PCE) in comparison with nonfunctional PCE and generic control double-stranded RNAs (dsRNAs). N-terminal domain exhibits higher binding affinity for PCE than for nonfunctional mutant RNA or control dsRNA. Highly conserved surface-exposed lysine residues are required for selective interaction with PCE RNA. In cells, the N-terminal domain directs interaction with PCE, mRNA and its exogenous expression blocks the translation activity of endogenous RHA Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens recombinant N-terminal, central helicase, and C-terminal domains of RHA are evaluated for their ability to specifically interact with cognate RNAs by in vitro biochemical measurements and mRNA translation assays in cells. Results demonstrate that N-terminal residues confer selective interaction with retroviral and junD target RNAs. Conserved lysine residues in the distal alpha-helix of the double-stranded RNA-binding domains are necessary to engage structural features of retroviral and junD 5'-UTRs ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using affinity chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information recombinant N-terminal, central helicase, and C-terminal domains of RHA are evaluated for their ability to specifically interact with cognate RNAs by in vitro biochemical measurements and mRNA translation assays in cells. Results demonstrate that N-terminal residues confer selective interaction with retroviral and junD target RNAs. Conserved lysine residues in the distal alpha-helix of the double-stranded RNA-binding domains are necessary to engage structural features of retroviral and junD 5'-UTRs Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
DExH protein RNA helicase A
-
 Homo sapiens
RHA
-
 Homo sapiens