Disease relevance of YMR262W

• The phosphorylated form of the ORF3 protein of hepatitis E virus interacts with its non-glycosylated form of the major capsid protein, ORF2 [1].
• The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK [2].
• Pseudomonas syringae pv. tomato DC3000 HopPtoM (CEL ORF3) is important for lesion formation but not growth in tomato and is secreted and translocated by the Hrp type III secretion system in a chaperone-dependent manner [3].

High impact information on YMR262W

• The predicted amino acid sequence of ORF3 has motifs characteristic of viral RNA-dependent RNA polymerases [4].
• The ORF3 protein of hepatitis E virus interacts with liver-specific alpha1-microglobulin and its precursor alpha1-microglobulin/bikunin precursor (AMBP) and expedites their export from the hepatocyte [5].
• Human liver cells showing co-localization of ORF3 with endogenously expressing alpha(1) m showed a distinct disappearance of the protein from the Golgi compartment, suggesting that ORF3 enhances the secretion of alpha(1)m out of the hepatocyte [5].
• ORF3 maps in the structural region of the HEV genome and now interacts with the major capsid protein, ORF2, in a post-translational modification-dependent manner [1].
• Although ORF3 alone is sufficient for MAK3 activity when expressed from an expression vector, in its native context an additional 669 base pairs 3' to the ORF and complementary to the gene for a non-histone protein are necessary for expression, but not for normal steady state transcript levels [6].

Biological context of YMR262W

• None of the plasmids contained the sequences homologous to ORF3 and ORF4 of pGKL1 encoding the toxin resistance determinant and the toxin gamma subunit, respectively [7].

Anatomical context of YMR262W

• Finally, (1)pulse labeling of alpha(1)m showed that its secretion was expedited out of the liver cell at faster rates in the presence of the ORF3 protein [5].

Analytical, diagnostic and therapeutic context of YMR262W

• Using fluorescence-based colocalization, yeast two-hybrid experiments, transiently transfected COS-1 cell co-immunoprecipitation, and cell-free coupled transcription-translation techniques, we have shown that the ORF3 protein interacts with the ORF2 protein [1].

References