Pelota (known as DOM34 in yeast) binds Hbs1, which is EF1-alpha-related subfamily GTPase, and is considered to play a crucial role in mRNA surveillance for protein synthesis []. It is involved in No-go decay (NGD) and non-stop decay (NSD) surveillance mechanisms that target mRNAs on which elongation complexes are stalled. Pelota/Hbs1 were shown to promote dissociation of stalled elongation complexes and release of intact peptidyl-tRNA in the presence of the ATP-binding cassette protein ABCE1 []. Pelota is conserved in eukaryotes and archaea [].
Pelota (known as DOM34 in yeast) binds Hbs1, which is EF1-alpha-related subfamily GTPase, andis considered to play a crucial role in mRNA surveillance for protein synthesis []. It is involved in No-go decay (NGD) and non-stop decay (NSD) surveillance mechanisms that target mRNAs on which elongation complexes are stalled. Pelota/Hbs1 were shown to promote dissociation of stalled elongation complexes and release of intact peptidyl-tRNA in the presence of the ATP-binding cassette protein ABCE1 []. Pelota is conserved in eukaryotes and archaea [].Dom34 and Pelota are organised in three domains. The N-terminal domain, annotated as domain A in Pelota [], represented by this entry, adopts a Sm-fold that is often involved in the recognition of mRNA stem loops or in the recruitment of mRNA degradation machinery [].
This entry represents the ABCE family of ATP-binding cassette (ABC) transporters and solely comprises of the ABCE1 gene product (also known as RNase L inhibitor, RLI1) [, , ]. RLI1 contains 2 nucleotide-binding domains (NBDs) typical of the ABC transporter protein superfamily []; however, it lacks the transmembrane domains required for membrane transport functions [, ]. RLI1 was first identified as an endoribonuclease inhibitor that interacts directly with RNase L to prevent it from binding 2-5A (5'-phosphorylated 2',5'-linked oligo- adenylates) []. RNase L plays a major role in the anti-viral and anti-proliferative activities ofinterferons, and its inhibition by RLI1 occurs in a concentration-dependent manner [, ]. Recently, RLI1 has been shown to be essential for the assembly of immature HIV-1 capsids in insect cells and higher eukaryotic cell types []. RLI1 expression is induced during HIV type I infection, and is understood to bind HIV-1 Gag (p55) polypeptides following their translation, and to promote their assembly into immature HIV-1 capsids [, , ].
