Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An intermediate in the ethidium bromide (EB) induced petite mutation pathway may be destabilized by daylight light to cause a reversion to the normal grande phenotype. Starved cells preincubated in the dark for up to 6 h with 100 microgram/ml EB could be reverted to grandes after one hour of light exposure, whereas similarly treated cells maintained in the dark expressed the petite mutation in more than 80 percent of the population. In addition, the production of petite mutants by EB in buffer could be prevented if cell suspensions were exposed to light immediately upon the addition of EB. Photoreversal of the EB-derived petite mutation in growing cells was less efficient presumably because the availability of an energy source caused a continuation of mutation events beyond the light revertible step to a non-reversible fixation of the mutation. Cells treated with EB in growth media at 4 degrees C were more responsive to light protection and reversal of the mutation. This may be due to the cold inhibition of an enzyme which comes into play beyond the light sensitive step in the mutation pathway.
Mol Gen Genet 1979 Jan 16
PMID:Reversal of protection by light of the ethidium bromide induced petite mutation in yeast. 37 99

Cold-sensitive mutants of Saccharomyces cerevisiae isolated by tritium suicide were screened for defects in ribosome biosynthesis. The biochemical defects of mutant dip-1 (defective in processing) were characterized; it is defective in ribosome biosynthesis at the level of production of the primary 35S transcript. At restrictive conditions mutant dip-1 accumulates abnormal rRNA in addition to wild-type rRNA. In the mutant the first observable transcription product was a 14SRNA species which had sequence homologies to 18S rDNA and was the major rRNA component of the 40S ribosomal subunit. In addition, the ribonucleoprotein particles of dip-1 harbored RNA molecules with homologies to yeast rDNA which comprises the spacer region between 18S and 25S rDNA cistrons. Possible causes for the defective production of rRNA and its assembly into subunits are discussed.
Mol Gen Genet 1979 Oct 01
PMID:A cold-sensitive mutant of Saccharomyces cerevisiae defective in ribosome processing. 39 31

Seven suppressor mutations have been isolated in Aspergillus nidulans by coreversion of alleles in physiologically unrelated genes namely, alX, sB, alcA, putative structural genes for allantoinase, sulphate permease and alcohol dehydrogenase respectively. The suppressors are allele specific, gene unspecific. Those described map in four loci, suaA, B, C, D. suaA and suaB are on linkage group III, suaC and suaD on VII. suaB111, suaD103 and suaD108 are semi-dominant in their suppression of alX4 and sB43, suaA101, suaA105 and suaC10. are recessive and have a pleiotropic effect on morphology. SuaC109 is cold sensitive for growth as is sua115, an unmapped mutation on linkage group III which is similar in morphology to suaC109. The two mutations, suaA101 and suaA105 have different spectra of suppression and morphologies. suaA105 weakly suppresses alX4 and sB43 whereas suaA101 strongly suppresses these and alcA125. suaD103 and suaD108 have the same spectrum of suppression. The properties of these suppressors are consistent with their being informational suppressors are consistent with their being informational suppressors of the nonsense type.
Mol Gen Genet 1979
PMID:Allele specific, gene unspecific suppressors in Aspergillus nidulans. 39 16

A cold-sensitive mutation in the rpoB gene for the RNA polymerase beta subunit increasing the temperature of promoter opening on T2 phage DNA was obtained in Escherichia coli. The mutation also affects the stages preceding promoter opening by increasing the dissociation rate of RNA polymerase--DNA closed complexes. The affinity of RNA polymerase to T2 and lambda DNA is differentially changed by the mutation. The relative efficiency of transcription of these two templates is also changed. These results suggest a participation of the RNA polymerase beta subunit in the interaction with promoters.
Mol Gen Genet 1979 Oct 02
PMID:A cold-sensitive beta subunit mutant RNA polymerase from Escherichia coli with defects in promoter opening in vitro. 39 44

A cold-sensitive mutation in Escherichia coli, affecting the beta-subunit of RNA polymerase and causing an increase in the temperature of promoter opening on T2 phage DNA, was obtained. The mutation also affects the stages preceding promoter opening by increasing the dissociation rate of RNA polymerase--DNA closed complexes. The affinity of RNA polymerase to T2- and lambda-DNA is differently changed by the mutation. The relative efficiency of transcription of these two templates is also changed. These results suggest a participation of the beta-subunit of RNA polymerase in the interaction with promoters.
Mol Biol (Mosk)
PMID:[Cold-sensitive mutation in the beta-subunit of Escherichia coli RNA polymerase affecting the opening of promoters]. 39 1

The three-dimensional crystal structure of bovine trypsinogen at approximately pH 7.5 was initially solved at 2.6 A resolution using the multiple isomorphous replacement method. Preliminary refinement cycles of the atomic coordinates trypsinogen have been carried out first to a resolution of 2.1 A, and later to 1.9 A, using constrained difference Fourier refinement; During the process, structure factors Fc and phi c were calculated from the trypsinogen structure and final interpretation was based on an electron-density map computed with terms (2 Fo - Fc) and phases phic at a resolution of 1.9 A. Crystals of trypsinogen grown from ethanol-water mixtures are trigonal with space group P3121, and cell dimension a = 55.17 A and c = 109.25 A. The structure is compared with the bovine diisopropylphosphoryltrypsin structure at approximately pH 7.2, oirginally determined from orthohombic crystals by Stroud et al. (Stroud, R.M., Kay L.M., and Dickerson, R.E. (1971), Cold Spring Harbor Symp. Quant. Biol. 36, 125-140; Stroud, R.M., Kay, L.M., and Dickerson, R.E. (1974), J. Mol. Biol. 83, 185-208), and later refined at 1.5 A resolution by Chambers and Stroud (Chambers, J.L., and Stroud, R.M. (1976), Acta Crystallogr. (in press)). At lower pH, 4.0-5.5 diogen, with cell dimensions a = 55.05 A and c = 109.45 A. This finding was used in the solution of the six trypsinogen heavy-atom derivatives prior to isomorphous phase analysis, and as a further basis of comparison between trypsinogen and the low pH trypsin structure. There are small differences between the two diisopropylphosphoryltrypsin structures. Bovine trypsinogen has a large and accessible cavity at the site where the native enzyme binds specific side chains of a substrate. The conformation and stability of the binding site differ from that found in trypsin at approximately pH 7.5, and from that in the low pH form of diisopropylphosphoryltrypsin. The catalytic site containing Asp-102, His-57, and Ser-195 is similar to that found in trypsin and contains a similar hydrogen-bounded network. The carboxyl group of Asp-194, which is salt bridged to the amino terminal of Ile-16 in native trypsin or other serine proteases, is apparently hydrogen bonded to internal solvent molecules in a loosely organized part of the zymogen structure. The unusually charged N-terminal hexapeptide of trypsinogen, whose removal leads to activation of the zymogen, lies on the outside surface of the molecule. There are significant structural changes which accompany activation in neighboring regions, which include residues 142-152, 215-550, 188A-195. The NH group of Gly-193, normally involved in stabilization of reaction intermediates (Steitz, T.A., Henderson, R., and Blow, D.M. (1969), J. Mol. Biol. 46, 337-348; Henderson, R. (1970), J. Mol. Biol. 54, 341-354; robertus, J.D., Kraut, J., Alden, R.A., and Birkoft, J.J. (1972), Biochemistry 11, 4293-4303) in the enzyme, is moved 1.9 A away from its position in trypsin...
 ...
PMID:Structure of bovine trypsinogen at 1.9 A resolution. 55 51

Mutants of Mucor mucedo minus strain that are affected in their trisporic acid (TA) mediated zygophore formation have been isolated. We have found mutants with cold sensitive (cs), with temperature sensitive (ts) and without zygophore formation as well as mutants with unstable zygophores (Zst-). From the appearence of certain pleiotropic phenotypes we deduce a one-dimensional sequence of states of competence of the mycelium to form different organs. TA appears to be a growth substance for zygophores acting on one transient state of competence. The fact that all isolates with lowered response to TA also have a lowered response to the mating type specific TA-precursor P strongly suggests that P has to be converted into TA before inducing zygophore growth. Furthermore, one mutant with lowered sensitivity to TA exhibits an excess zygophore formation in the presence of high TA-concentrations, while high concentrations of P cause a depressed zygophore formation (Fig. 6). Our interpretation of this behaviour is that P acts as an antagonist to TA in the regulation of zygophore growth.
Mol Gen Genet 1978 Feb 27
PMID:Morphogenesis in Mucor mucedo: mutations affecting gamone response and organ differentiation. 63 77

Six UV induced cycloheximide-sensitive revertants were isolated from the cyh1-C7 strain of Schizosaccharomyces pombe which is resistant to cycloheximide. In all cases reversion to sensitivity was due to a forward mutation in a second suppressor gene. Genetical analysis showed that at least two genes, designated scr1 and scr2 (scr=suppression of cycloheximide resistance) were involved. Both scr1 and scr2 suppressed the resistance of six independently isolated alleles at the cyh1 locus. They had no effect on two known nonsense mutations in the ade7 locus. The cyh1-C7 strain has an altered 60S ribosomal protein which can be detected by two-dimensional polyacrylamide gel electrophoresis. In two suppressed strains, cyh1-C7 scr1 and cyh1-C7 scr2, the original altered protein was present. However no further ribosomal protein differences were observed which could be correlated with the presence of the scr genes. Both scr mutations conferred cold sensitivity on the organism indicating that they were of the missense type. Hence it seems certain that scr1 and scr2 are not mutations in tRNA genes leading to either nonsense or missense suppression. There is however no direct evidence that they code for ribosomal proteins and exert their effect on cyh1-C7 at the ribosomal level.
Mol Gen Genet 1978 Jun 14
PMID:Genetical studies on revertants to sensitivity from a cycloheximide resistant strain of Schizosaccharomyces pombe. 67 2

1. In eight patients with a unilateral fistula between the radial artery and a nearby superficial vein, heat elimination from both hand and forearm, as measured by calorimetry, was always substantially greater on the side of the fistula (a mean excess from hand-plus-forearm 889 J/min). 2. Fistular blood flow measured by hand-plus-forearm plethysmography in these patients averaged 431ml/min. Correlation between fistular blood flow and heat elimination was poor (r = 0.70, P less than 0.06), probably because heat elimination due to the fistula takes place mainly from veins, whose pattern varies from patient to patient. 3. Approximately half of the total increased heat elimination due to the fistula is from the hand. Occlusion of the circulation to the hand caused fistular flow rate to be reduced by about half. This suggests that the main resistance to fistular is venous, proximal veins offering a similar resistance to distal veins. 4. The obligatory heat loss due to fistula is unlikely to embarrass temperature regulation, except in severe cold stress.
Clin Sci Mol Med 1978 Oct
PMID:Effect of a surgically created side-to-side arteriovenous fistula on heat elimination from the human hand and forearm: evidence for a critical role of venous resistance in determining fistular flow. 71 50

A double mutant strain combining two ribosomal mutations conferring resistance to cycloheximide exhibits a cold-sensitive phenotype. At low temperature the biosynthesis of the 60S subunit is impaired. Genetic analysis of cold-resistant revertants have shown that this double mutant strain can be used efficiently to isolate new ribosomal mutations.
Mol Gen Genet 1978 Oct 24
PMID:Cold-sensitivity of a double mutant strain combining two ribosomal mutations in the ascomycete Podospora anserina. 73 74


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