Regulation of amino acid synthetic enzymes in Neurospora crassa in the presence of high concentrations of amino acids

1986 ◽  
Vol 203 (3) ◽  
pp. 533-537 ◽  
Author(s):  
Ilse B. Barthelmess
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Neurospora Crassa ◽  
Synthetic Enzymes ◽  
High Concentrations

scholarly journals Sequence and structure of mtr, an amino acid transport gene of Neurospora crassa

Genome ◽  
1991 ◽  
Vol 34 (4) ◽  
pp. 644-651 ◽  
Author(s):  
Kenneth Koo ◽  
W. Dorsey Stuart
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Neurospora Crassa ◽  
Rna Binding ◽  
Signal Sequence ◽  
Average Length ◽  
Open Reading Frame ◽  
Mrna Transcript ◽  
S1 Nuclease ◽  
Reading Frame

The gene product of the mtr locus of Neurospora crassa is required for the transport of neutral aliphatic and aromatic amino acids via the N system. We have previously cloned three cosmids containing Neurospora DNA that complement the mtr-6(r) mutant allele. The cloned DNAs were tightly linked to restriction fragment length polymorphisms that flank the mtr locus. A 2.9-kbp fragment from one cosmid was subcloned and found to complement the mtr-6(r) allele. Here we report the sequence of the fragment that hybridized to a poly(A)+ mRNA transcript of about 2300 nucleotides. We have identified an 845-bp open reading frame (ORF) having a 59-bp intron as the potential mtr ORF. S1 nuclease analysis of the transcript confirmed the transcript size and the presence of the intron. A second open reading frame was found upstream in the same reading frame as the mtr ORF and appears to be present in the mRNA transcript. The mtr ORF is predicted to encode a 261 amino acid polypeptide with a molecular mass of 28 613 Da. The proposed polypeptide exhibits six potential α-helical transmembrane domains with an average length of 23 amino acids, does not have a signal sequence, and contains amino acid sequence homologous to an RNA binding motif.Key words: sequence, membranes, ribonucleoprotein.

Molecular analysis of nuc-1+, a gene controlling phosphorus acquisition in Neurospora crassa

1990 ◽  
Vol 10 (11) ◽  
pp. 5839-5848
Author(s):  
S Kang ◽  
R L Metzenberg
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurospora Crassa ◽  
Phosphorus Acquisition ◽  
Regulatory Factor ◽  
Physical Interactions ◽  
Negative Regulatory Factor ◽  
High Phosphate

In response to phosphorus starvation, Neurospora crassa makes several enzymes that are undetectable or barely detectable in phosphate-sufficient cultures. The nuc-1+ gene, whose product regulates the synthesis of these enzymes, was cloned and sequenced. The nuc-1+ gene encodes a protein of 824 amino acids with a predicted molecular weight of 87,429. The amino acid sequence shows homology with two yeast proteins whose functions are analogous to that of the NUC-1 protein. Two nuc-1+ transcripts of 3.2 and 3.0 kilobases were detected; they were present in similar amounts during growth at low or high phosphate concentrations. The nuc-2+ gene encodes a product normally required for NUC-1 function, and yet a nuc-2 mutation can be complemented by overexpression of the nuc-1+ gene. This implies physical interactions between NUC-1 protein and the negative regulatory factor(s) PREG and/or PGOV. Analysis of nuc-2 and nuc-1; nuc-2 strains transformed by the nuc-1+ gene suggests that phosphate directly affects the level or activity of the negative regulatory factor(s) controlling phosphorus acquisition.

scholarly journals Molecular analysis of nuc-1+, a gene controlling phosphorus acquisition in Neurospora crassa.

1990 ◽  
Vol 10 (11) ◽  
pp. 5839-5848 ◽  
Author(s):  
S Kang ◽  
R L Metzenberg
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurospora Crassa ◽  
Phosphorus Acquisition ◽  
Regulatory Factor ◽  
Physical Interactions ◽  
Negative Regulatory Factor ◽  
High Phosphate

In response to phosphorus starvation, Neurospora crassa makes several enzymes that are undetectable or barely detectable in phosphate-sufficient cultures. The nuc-1+ gene, whose product regulates the synthesis of these enzymes, was cloned and sequenced. The nuc-1+ gene encodes a protein of 824 amino acids with a predicted molecular weight of 87,429. The amino acid sequence shows homology with two yeast proteins whose functions are analogous to that of the NUC-1 protein. Two nuc-1+ transcripts of 3.2 and 3.0 kilobases were detected; they were present in similar amounts during growth at low or high phosphate concentrations. The nuc-2+ gene encodes a product normally required for NUC-1 function, and yet a nuc-2 mutation can be complemented by overexpression of the nuc-1+ gene. This implies physical interactions between NUC-1 protein and the negative regulatory factor(s) PREG and/or PGOV. Analysis of nuc-2 and nuc-1; nuc-2 strains transformed by the nuc-1+ gene suggests that phosphate directly affects the level or activity of the negative regulatory factor(s) controlling phosphorus acquisition.

Effect of fertilization on free amino acid concentrations in black spruce and jack pine containerized seedlings

1987 ◽  
Vol 17 (1) ◽  
pp. 27-30 ◽  
Author(s):  
Y. T. Kim ◽  
C. Glerum ◽  
J. Stoddart ◽  
S. J. Colombo
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Free Amino ◽  
Black Spruce ◽  
Jack Pine ◽  
Foliar Nitrogen ◽  
Containerized Seedlings ◽  
High Concentrations ◽  
Amino Acid Concentrations

Greenhouse-grown black spruce and jack pine container seedlings were fertilized weekly with a 20–8–20 fertilizer at four concentrations during the fall. Seedlings were sampled when 23 weeks old towards the end of the greenhouse cultural period to determine the effect of fertilization on the free amino acid concentrations. All amino acids, except tryptophan, showed significant increases in concentration with higher levels of fertilizer; the concentration of tryptophan decreased with increasing fertilizer concentration. Amino acids with the highest concentrations in black spruce were arginine, glutamic acid, and proline, while in jack pine, besides these three, aspartic acid and glutamine were also found in high concentrations. Black spruce had significantly higher amino acid concentrations than jack pine. The concentrations of certain free amino acids may be more sensitive indicators of seedling nitrogen status than total foliar nitrogen.

Adaptational changes in Staphylococcus aureus MF31 grown above its maximum temperature when protected by NaCl: physiological studies

1984 ◽  
Vol 30 (9) ◽  
pp. 1105-1111 ◽  
Author(s):  
A. Hurst ◽  
Esther Ofori ◽  
A. A. El-Banna ◽  
J. Harwig
Keyword(s):  
Amino Acids ◽  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Monosodium Glutamate ◽  
Amino Acid Pool ◽  
Maximum Temperature ◽  
C Cells ◽  
Acid Pool ◽  
High Concentrations ◽  
P Cells

Staphylococcus aureus MF31 can grow at 46 °C, 2 °C above its normal maximum temperature of growth if 1 M NaCl is added to the medium. In the present work we show that monosodium glutamate, proline, threonine, aspartic acid, and betaine (in order of decreasing effectiveness) also enabled cells to grow at 46 °C. Cells grown at 46 °C in he presence of salt (protected or P cells) accumulated glutamate more rapidly than cells grown at 37 °C without salt (normal or N cells) and contained an increased amino acid pool. The principal constituents of this pool were dicarboxylic amino acids and proline. Turbidimetric evidence suggests that NaCl caused plasmolysis in S. aureus. The P cells, although grown in 1 M NaCl, had about the same Cl− and K+ content as the N cells grown without added NaCl. P cells had increased heat resistance but high concentrations of CaCl2 in the heating menstruum reduced their D55 value from a maximum of 214 min to < 30 s. We suggest that growth at 46 °C in 1 M NaCl can be explained, in part at least, by the increased amino acid pool internal to the cell and the external osmotic support given by Cl− anions excluded by the cell.

ESSENTIAL AMINO ACIDS IN MICROORGANISMS

1957 ◽  
Vol 3 (5) ◽  
pp. 721-728 ◽  
Author(s):  
F. Reusser ◽  
J. F. T. Spencer ◽  
H. R. Sallans
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Quantitative Method ◽  
Essential Amino Acids ◽  
Cellular Protein ◽  
One Dimensional ◽  
Low Concentrations ◽  
Amino Acid Determination ◽  
High Concentrations ◽  
Acid Determination

The cells of 19 species of bacteria, actinomyces, and yeasts were analyzed for protein and essential amino acids. A rapid quantitative method for amino acid determination using one-dimensional paper chromatography was developed. The cellular protein from all species contained relatively high concentrations of lysine, somewhat lower concentrations of tryptophan and threonine, and very low concentrations of methionine. All of the 10 essential amino acids were found in each species tested, although individual differences in the relative and absolute amounts were observed.

Large enhancement of canine taste responses to amino acids by salts

1993 ◽  
Vol 264 (6) ◽  
pp. R1071-R1076 ◽  
Author(s):  
T. Ugawa ◽  
K. Kurihara
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Chorda Tympani ◽  
Chorda Tympani Nerve ◽  
Sodium Potassium ◽  
Calcium Salts ◽  
Receptor Sites ◽  
Large Enhancement ◽  
Magnesium Salts ◽  
High Concentrations

The effects of salts on the canine taste responses to amino acids were examined by recording the activity of the chorda tympani nerve. 1) The tonic responses to most amino acids examined were significantly enhanced by the presence of various salts. 2) The degree of the enhancement varied with the species of amino acid and salt. The responses to most amino acids were enhanced by sodium, potassium, and calcium salts, but not enhanced by magnesium salts. The response to methionine, for example, was enhanced by NaCl, but not by Na phosphate of equimolar Na+. 3) The responses to glycine and alanine were suppressed by high concentrations of NaCl. 4) The presence of salts (NaCl and CaCl2) enhanced the responses to amino acids without affecting the thresholds for the amino acids, suggesting that the presence of the salts did not change the affinity of amino acids to the receptor sites. 5) The enhancing effects of salts on the responses to amino acids could not be explained in terms of permeability of cation and anion of salts. It was speculated that the binding of cation and anion of salts on the receptor membranes induces exposure of the receptor sites for amino acids available for binding of amino acids.

cpc-2, a new locus involved in general control of amino acid synthetic enzymes in Neurospora crassa

1990 ◽  
Vol 18 (3) ◽  
pp. 211-215 ◽  
Author(s):  
Dirk Kr�ger ◽  
Jutta Koch ◽  
Ilse B. Barthelmess
Keyword(s):  
Amino Acid ◽  
Neurospora Crassa ◽  
General Control ◽  
Synthetic Enzymes

scholarly journals Carbohydrate content of insoluble elastins prepared from adult bovine and calf ligamentum nuchae and tropoelastin isolated from copper-deficient procine aorta

1971 ◽  
Vol 121 (2) ◽  
pp. 197-202 ◽  
Author(s):  
M. E. Grant ◽  
F. S. Steven ◽  
D. S. Jackson ◽  
L. B. Sandberg
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Carbohydrate Content ◽  
Amino Sugars ◽  
Collagenase Digestion ◽  
Low Concentrations ◽  
Neutral Sugars ◽  
High Concentrations ◽  
Edta Extraction

1. Insoluble elastin has been prepared by several different methods from adult bovine and calf ligamentum nuchae. Highly purified tropoelastin has been prepared from copper-deficient porcine aorta. 2. Amino acid analyses indicated that all preparations, except that obtained from calf ligamentum nuchae by using an EDTA extraction followed by collagenase digestion (preparation E6), were typical of pure elastin having high concentrations of hydrophobic and low concentrations of hydrophilic amino acids. Preparation E6 was found to contain approx. 40% collagen. 3. The determination and composition of the carbohydrates associated with these preparations is reported. With the exception of preparation E6, the insoluble elastins contained only trace amounts of neutral sugars (0.13–0.35%, w/w) and amino sugars (0.01–0.06%, w/w). The porcine tropoelastin contained virtually no carbohydrate. 4. The results suggest that carbohydrate analyses can yield valuable information about the purity of elastin preparations.

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