Constitutive Synthesis of Enzymes Involved in 2-Aminophenol Metabolism and Inducible Synthesis of Enzymes Involved in Benzoate,p-Hydroxybenzoate, and Protocatechuate Metabolism inPseudomonassp. Strain AP-3

2005 ◽  
Vol 69 (5) ◽  
pp. 1033-1035 ◽  
Author(s):  
Shinji TAKENAKA ◽  
Endang SETYORINI ◽  
Young-Ju KIM ◽  
Shuichiro MURAKAMI ◽  
Kenji AOKI

1997 ◽  
Vol 17 (11) ◽  
pp. 6303-6310 ◽  
Author(s):  
L Yu ◽  
M A Gorovsky

Although quantitatively minor replication-independent (replacement) histone variants have been found in a wide variety of organisms, their functions remain unknown. Like the H3.3 replacement variants of vertebrates, hv2, an H3 variant in the ciliated protozoan Tetrahymena thermophila, is synthesized and deposited in nuclei of nongrowing cells. Although hv2 is clearly an H3.3-like replacement variant by its expression, sequence analysis indicates that it evolved independently of the H3.3 variants of multicellular eukaryotes. This suggested that it is the constitutive synthesis, not the particular protein sequence, of these variants that is important in the function of H3 replacement variants. Here, we demonstrate that the gene (HHT3) encoding hv2 or either gene (HHT1 or HHT2) encoding the abundant major H3 can be completely knocked out in Tetrahymena. Surprisingly, when cells lacking hv2 are starved, a major histone H3 mRNA transcribed by the HHT2 gene, which is synthesized little, if at all, in wild-type nongrowing cells, is easily detectable. Both HHT2 and HHT3 knockout strains show no obvious defect during vegetative growth. In addition, a mutant with the double knockout of HHT1 and HHT3 is viable while the HHT2 HHT3 double-knockout mutant is not. These results argue strongly that cells require a constitutively expressed H3 gene but that the particular sequence being expressed is not critical.



1992 ◽  
Vol 12 (7) ◽  
pp. 2958-2966
Author(s):  
M Bun-Ya ◽  
S Harashima ◽  
Y Oshima

We have found an open reading frame which is 1.1 kb upstream of PHO84 (which encodes a Pi transporter) and is transcribed from the opposite strand. In Saccharomyces cerevisiae, this gene is distal to the TUB3 locus on the left arm of chromosome XIII and is named GTR1. GTR1 encodes a protein consisting of 310 amino acid residues containing, in its N-terminal region, the characteristic tripartite consensus elements for binding GTP conserved in GTP-binding proteins, except for histidine in place of a widely conserved aspargine residue in element III. Disruption of the GTR1 gene resulted in slow growth at 30 degrees C and no growth at 15 degrees C; other phenotypes resembled those of pho84 mutants and included constitutive synthesis of repressible acid phosphatase, reduced Pi transport activity, and resistance to arsenate. The latter phenotypes were shown to be due to a defect in Pi uptake, and the Gtr1 protein was found to be functionally associated with the Pho84 Pi transporter. Recombination between chromosome V (at the URA3 locus) and chromosome XIII (in the GTR1-PHO84-TUB3 region) by using a plasmid-encoded site-specific recombination system indicated that the order of these genes was telomere-TUB3-PHO84-GTR1-CENXIII.



Author(s):  
L. A. Chudinova ◽  
◽  
D. R. Yusupov ◽  

We studied the growth rate of rye seedlings, as well as the dynamics of the content of soluble proteins and proline in the shoots during their adaptation to sharp (300 mM NaCl once, exposure time 9 days) and gradual (100 mM NaCl, then 100 mM NaCl after 2 days to the final concentration of 400 mM) salinity with sodium chloride in the presence or absence of thermal hardening (+40°C, 3 h). The established dy-namics of the content of proline and soluble proteins in the shoots suggests that the formation of re-sistance to salinity is determined by the high constitutive level of proline, as well as the stress-inducible synthesis of proline and water-soluble proteins. Thermal pretreatment of the seedlings stimulated their constitutive stability to a greater extent. The detected metabolic changes are obviously related to one of the possible mechanisms of the protective effect of thermal hardening on subsequent salinization.



1983 ◽  
Vol 3 (1) ◽  
pp. 70-81 ◽  
Author(s):  
C D Scher ◽  
R L Dick ◽  
A P Whipple ◽  
K L Locatell

The platelet-derived growth factor (PDGF) stimulates density-arrested BALB/c-3T3 cells to synthesize a protein (pII; Mr, 35,000) that is constitutively synthesized by spontaneously transformed BALB/c-3T3 (ST2-3T3) cells which do not require PDGF for growth. Antisera against a major excreted protein family (MEP) of retrovirus-transformed cells quantitatively precipitated cellular pII. PDGF-stimulated pII has the same molecular weight, a similar charge, and similar antigenic determinants as authentic MEP isolated from ST2-3T3 or retrovirus-transformed cells. MEP represented about 2% of the nonnuclear proteins synthesized by ST2-3T3 cells and 0.3 to 0.6% of the proteins synthesized by PDGF-treated BALB/c-3T3 cells, a three- to sixfold increase over the background. In BALB/c-3T3 cells, less PDGF was required for pII (MEP) synthesis than for DNA synthesis. PDGF induced a selective increase in pII (MEP) within 40 min. Such preferential synthesis was inhibited by brief treatment with actinomycin D, suggesting a requirement for newly formed RNA. The constitutive synthesis of pII (MEP) by ST2-3T3 cells was not inhibited by actinomycin D. Five spontaneously or chemical carcinogen-transformed tumorigenic BALB/c-3T3 cell lines were studied; they neither required PDGF for growth nor responded to it. These cell lines became arrested at confluence with a G1 DNA content. Each of these independently isolated lines synthesized pII (MEP) constitutively. Thus, the synthesis of pII (MEP) may be required, but is not sufficient, for PDGF-modulated DNA synthesis.



1986 ◽  
Vol 6 (2) ◽  
pp. 71-77 ◽  
Author(s):  
ANNE-CATHERINE PASSAQUIN ◽  
GILLIANE COUPIN ◽  
PHILIPPE POINDRON




Virology ◽  
1992 ◽  
Vol 189 (2) ◽  
pp. 812-816 ◽  
Author(s):  
L. Ottavio ◽  
O. Sthandier ◽  
L. Ricci ◽  
C. Passananti ◽  
P. Amati


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