Regulation of Protein Synthesis

Vogel, Henry J.; Vogel, Ruth H.

doi:10.1146/annurev.bi.36.070167.002511

Cited by 67 publications

(11 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…There is evidence for the existence of a regulator gene in the latter organism. Induction of barley root nitrate reductase by its substrate, nitrate, and partial inhibition of this induction by an eventual product, ammonium, suggests that higher plants may control flow through some metabolic pathways by mechanisms similar to those that have been described for microorganisms (10,33). However, since only partial inhibition of enzyme synthesis was observed and since ammonium did not reduce the amount of nitrate reduced (Table III), it appears that the control is not as tight in higher plants at it is in microorganisms.…”

Section: Discussionmentioning

confidence: 86%

See 1 more Smart Citation

Regulation of Nitrate Reductase in Excised Barley Roots

Smith

Thompson

1971

Plant Physiol.

View full text Add to dashboard Cite

(15); pH 7.5. To inhibit nitrification, 2-chloro-6-(trichloromethyl) pyridine ("Nserve," Dow Chemical Company, Midland, Mich.)' (1 jug/ml) was added. The seedlings grew another 24 hr in darkness prior to harvest.The roots from these seedlings were then thoroughly rinsed with distilled water, excised just below the screen, and suspended in a large volume of aerated distilled water. After the roots were blotted dry, 1-g samples were weighed out and transferred to 40-X 200-mm test tubes containing distilled water. The roots were rinsed twice more with sterile distilled water before being used.Incubation Treatment. Roots were incubated in sterile, aerated solutions for 6 hr at 25 to 28 C. The basal incubation medium contained: MgSO4, 0.38 mM; Na2HPO4, 0.33 mM; K2S04, 0.50 mM; CaC12, 1.00 mM; FeNaEDTA, 0.10 mM; trace elements (15), glucose 1% (w/v); pH 7.15. The addition of glucose was necessary to obtain a nitrate reductase increase. However, the inhibition of nitrate reductase increase by ammonium (see "Results and Discussion") was not due to inhibition of glucose absorption by ammonium. Using radioactive glucose, it was observed that ammonium did not affect glucose uptake at several glucose concentrations when nitrate reductase increased. Nitrate, ammonium, inhibitors, and other test compounds were added to the basal incubation medium as indicated in tables and figures. All treatments were run in duplicate and duplicates agreed closely. In each experiment, additional samples of roots were assayed for nitrate reductase activity at the beginning of the 6-hr incubation period. These samples have been identified as "zero induction time controls". After incubation, the roots were rinsed three times with deionized water, blotted, and cooled to 4 C.

show abstract

Section: Discussionmentioning

confidence: 86%

“…Metabolite levels and metabolic pathways in microorganisms are often controlled by regulating the synthesis or the activity of the enzymes involved in biosynthetic pathways (2,10,33). Evidence for similar mechanisms in higher plants is much less.…”

mentioning

confidence: 99%

Regulation of Nitrate Reductase in Excised Barley Roots

Smith

Thompson

1971

Plant Physiol.

View full text Add to dashboard Cite

show abstract

“…In addition to protein stability, the low abundance of a protein has been attributed to translational regulation of its transcript via the 5¢-UTR [17]. To investigate whether this might be a cause of the low abundance of MBP-1 in cells, we generated three plasmids: one with the MBP-1 ORF insert only (MBP-1 ⁄ ORF); one with the full-length MBP-1 cDNA (MBP-1 ⁄ FL); and one with the full-length cDNA lacking the first 206 nucleotides (MBP-1 ⁄ s-UTR).…”

Section: Protein Synthesis Of Mbp-1 Is Tightly Regulatedmentioning

confidence: 99%

MBP‐1 is efficiently encoded by an alternative transcript of the ENO1 gene but post‐translationally regulated by proteasome‐dependent protein turnover

et al. 2010

View full text Add to dashboard Cite

The c‐myc promoter‐binding protein‐1 (MBP‐1) is a transcriptional suppressor of tumorigenesis and thought to be the product of alternative translation initiation of the α‐enolase (ENO1) transcript. In the present study, we cloned a 2552‐bp novel cDNA with a putative coding sequence of MBP‐1 and functionally examined its ability to encode the MBP‐1 protein. Similarly to ENO1, the obtained MBP‐1 was widely and differentially expressed in a variety of normal tissues and cancer cells. Experiments using MBP‐1 promoter‐driven luciferase reporter assays, biochemical cell fractionation followed by RT‐PCR detection of the cytoplasmic mRNA, and transcription/translation‐coupled reactions, consistently demonstrated that this novel transcript was alternatively transcribed from intron III of the ENO1 gene and was feasible for MBP‐1 production. Hypoxia treatments significantly increased the transcriptional activation of the MBP‐1 gene. Blocking the proteasomal degradation by MG132 stabilized the MBP‐1 protein in cells. Compared with the translation efficiency for production of the MBP‐1 protein, the MBP‐1 transcript was 17.8 times more efficient than the ENO1 transcript. Thus, we suggest that this newly discovered transcript is a genuine template for the protein synthesis of MBP‐1 in cells, and optimal expression of this gene in tumors may lead to effective clinical therapies for cancers.

show abstract

“…From tlaese studies it is clear that histidyl tRNA is also involved in repression of the histidine operon. While such an observation does not eliminate an operator-repressor model in which it is the histidyl tRiVA ra!.her than free hlstidine which activates the repressor, it does invite speculation that repression is coupled directly to translation rather than to transcription, such as the mechanism suggested by Roth et al (110) or by the Vogel (185).…”

Section: Regulation Of Histidine Metabolismmentioning

confidence: 97%