Disease relevance of MTRF1

• The effects of tRNA, RF1 and RRF on trans-translation by tmRNA were examined using a stalled complex of ribosome prepared using a synthetic mRNA and pure Escherichia coli translation factors [1].
• By immunohistochemistry, normal human breast and prostate epithelium was negative for the major isoform [reading frame-1 (RF1)] of PEG10 protein, but this cytoplasmic protein was strongly expressed in a subset of breast carcinomas in situ and invasive ductal carcinomas ( approximately 30%) and in a similar percentage of prostate cancers [2].
• To determine the genetic and molecular basis for rheumatoid factor (RF) autoantibody reactivity in patients with destructive, erosive arthritis, we established a human lymphoblastoid cell line (hRF-1) from a patient with polyarthritis that produced an IgG RF mAb, mAb hRF-1 [3].
• A cloned lymphoblast cell line, hRF-1, that secreted human monoclonal IgG4 rheumatoid factor autoantibody was produced by Epstein-Barr virus transformation of lymphocytes from rheumatoid arthritis synovium [4].
• In B cell chronic lymphocytic leukemia (B-CLL), the pattern of D-RF was 25% for RF1, 46% for RF2 and 29% for RF3, while in B cell precursor acute lymphoblastic leukemia (precursor-B-ALL) all three RFs were used with similar frequencies [5].

Psychiatry related information on MTRF1

• Characteristics of this assay in terms of reaction time, ion concentration, release factor RF1 and RF2 concentration, and competition with A-site-decoding tRNA are discussed [6].

High impact information on MTRF1

• RF1 and RF2 exhibit significant sequence homology, probably reflecting their similar functions and perhaps a common evolutionary origin [7].
• Functional sites of interaction between release factor RF1 and the ribosome [8].
• Thus, RF1 and RF2 function like molecular machines, most likely fueled by histidine protonation [9].
• Ribosomal binding site of release factors RF1 and RF2. A new translational termination assay in vitro [6].
• To determine the molecular basis of this particular RF reactivity, the heavy and light chain genes of mAb hRF-1 were amplified by PCR, cloned, and ligated into the pSG5 plasmid for expression in COS-7 cells [10].

Biological context of MTRF1

• The L chain gene was cloned from a cDNA library prepared from hRF-1 cells [3].
• Elaboration of the RF1 synthesis in an effort to enhance the Zn(2+) affinity was unsuccessful, so palladium-catalyzed aryl amination was applied to prepare RF2 (1-[9'-(o-carboxyphenyl)-6'-amino-2'-chloro-3'-xanthanone]-4,10-(diethyl)-7-(2-pyridylmethyl)-1,4,7,10-tetraazacyclododecane, Rhodafluor-2) [11].
• Here we used cDNA microarrays to examine the different gene expression profiles of a primary gastric adenocarcinoma cell line RF1 and its derivative metastasis subline RF48 [12].

Anatomical context of MTRF1

• Identification and cloning of human mitochondrial translational release factor 1 and the ribosome recycling factor [13].
• Dihydrofolate reductase (DHFR) with an amber mutation was translated in the RF1-diminished prokaryotic cell free translation system in the presence of chemically-misacylated yeast tRNA(Phe)CUA [14].

Associations of MTRF1 with chemical compounds

• Here we have mapped the interaction of bacterial release factor RF1 with the ribosome by directed hydroxyl radical probing [8].
• RF1 is comprised of a fluorescein reporter coupled to a disulfide/dithiol switch [15].
• It was also shown that extension of puromycin on its 5'-hydroxyl end by up to ten deoxyoligonucleotides also allowed conjugation with the C terminus of in vitro translated protein when RF1-dependent termination was suppressed [16].
• A new class of ratiometric Zn(2+) sensors that employ a hybrid fluorescein and rhodamine fluorophore has been designed, and two members of the rhodafluor family of sensors, RF1 and RF2, have been synthesized [11].
• Comparing gene expression patterns of untreated RF1, untreated RF48 and treated RF48 cells showed 5 genes expressed in RF1 but silenced in RF48, which were reactivated after 5-aza-2'-deoxycytidine treatment [12].

Analytical, diagnostic and therapeutic context of MTRF1

• Confocal microscopy experiments show that RF1 can visualize multiple cycles of oxidation and reduction within living cells, establishing the potential value of this approach for probing dynamic oxidation biology events in natural systems [15].
• METHODS: Free radical activity was detected with a supercoiled plasmid, phi X174 RF1 DNA, and measured as scission of the supercoiled DNA (mediated by free radicals) by scanning laser densitometry [17].
• Northern blot analysis showed that this clone is expressed at a much higher level in the metastatic (RF48) than the nonmetastatic (RF1) cancer cell line from the same patient [18].
• The results show that RF1 and RF2 with an MIC(90) ( minimum -inhibitory concentration against 90% of the isolates) of 535.5 and 317 microg/mL respectively, performed generally better than TCN and AMP with an MIC(90) of 976.5 and 357 microg/mL respectively [19].

References