Disease relevance of TRNAS1

• On the basis of these experiments, TRS1 and IRS1 are proposed to be important intermediaries in the cascade of cytomegalovirus gene expression [1].
• Human cytomegalovirus TRS1 protein is required for efficient assembly of DNA-containing capsids [2].
• Our analysis of the ADsubTRS1 phenotype indicates that the TRS1 protein is required, either directly or indirectly, for efficient assembly of virus particles [3].
• Human cytomegalovirus TRS1 and IRS1 gene products block the double-stranded-RNA-activated host protein shutoff response induced by herpes simplex virus type 1 infection [4].
• Recombinant HSV-1 viruses expressing either the HCMV TRS1 or IRS1 protein demonstrate that either of these HCMV gene products allows the deltagamma1 34.5 recombinant viruses to evade PKR-mediated protein shutoff and maintain late viral protein synthesis [4].

High impact information on TRNAS1

• A similar phenomenon is also observed in mouse fibroblasts expressing a previously characterized iron-regulated human TfR mRNA (TRS-1) [5].
• Like the human cytomegalovirus dsRNA-binding protein genes TRS1 and IRS1, m142 and m143 are members of the US22 gene family [6].
• The fragment comprises the 3' end of the J1S open reading frame through the entire TRS1 gene [7].
• The addition in trans of the IRS1(263) protein, which antagonizes the ability of IRS1 and TRS1 proteins to activate reporter genes, did not inhibit the growth of the mutant virus [3].
• In transfection experiments pIRS1 and pTRS1 modestly activated expression from a reporter plasmid containing the viral major immediate-early promoter but did not influence the activity of a reporter carrying the irs1/trs1 immediate-early promoter [8].

Biological context of TRNAS1

• TRS1 is highly homologous to IRS1, which is encoded from the other copy of the c repeat, and plasmid constructs carrying the irs1 gene were also able to mediate transactivation of the ICP36 promoter [1].
• TRS1 is a member of the US22 family of proteins and is encoded by a region near the L-S junction of the viral genome within the c repeat and adjacent Us sequences [1].
• Proteins from UL112-113 and IRS1/TRS1, recently identified as essential loci for transient complementation of HCMV oriLyt-dependent DNA replication, were found to function as transactivators of the UL54 promoter in association with MIE proteins [9].
• RNA blot analysis of steady-rate RNA throughout infection showed that the trs1 transcript was expressed with the kinetics of an alpha gene but its accumulation was delayed relative to that of ie1 and ie2 transcripts [1].
• A total of 67 strains of T. rubrum were screened for genetic variation by randomly amplified polymorphic DNA (RAPD) analysis, with two primers, 5'-d[GGTGCGGGAA]-3' and 5'-d[CCCGTCAGCA]-3', as well as by subrepeat element analysis of the nontranscribed spacer of rDNA, using the repetitive subelements TRS-1 and TRS-2 [10].

Other interactions of TRNAS1

• Molecular characterization of the T. rubrum ribosomal DNA nontranscribed-spacer region revealed two novel tandemly repetitive subelements (TRSs): TRS-1, containing a 27-bp palindromic sequence, and TRS-2 [11].

Analytical, diagnostic and therapeutic context of TRNAS1

• Specific amplification of TRS-1 produced strain-characteristic banding patterns (PCR types), with 21 TRS-1 PCR types recognized from 101 clinical isolates [11].

References