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

Alterations in the pattern of polypeptide synthesis resulting from amino acid limitation in Neurospora crassa

1988 ◽  
Vol 34 (10) ◽  
pp. 1166-1170 ◽  
Author(s):  
Harry J. Flint ◽  
Janis McKormick
Keyword(s):  
Amino Acid ◽  
Neurospora Crassa ◽  
Two Dimensional ◽  
Wild Type ◽  
Supply Rate ◽  
Limited Growth ◽  
Synthetic Enzymes ◽  
Two Dimensional Electrophoresis ◽  
Polypeptide Synthesis ◽  
Dimensional Electrophoresis

Two-dimensional electrophoresis was used to examine the pattern of polypeptide synthesis in Neurospora crassa mycelium of an arg-6 strain grown in the presence of [14C]arginine. Reduction in the arginine supply rate led to amino acid limited growth, and to major alterations in the pattern of polypeptide synthesis. Strains carrying wild-type (cpc-1+) or mutant (cpc-1) alleles at a locus governing cross-pathway control of amino acid synthetic enzymes differed markedly with respect to their pattern of polypeptide synthesis under limitation conditions, but differed little during arginine sufficient growth. Among 160 abundant polypeptide species classified for their response to limitation in two dimensional fluorographs, 31 were induced by limitation only in a cpc-1+ strain, 13 only in a cpc-1 strain, and 9 showed induction in both strains.

Structure of the yeast HIS5 gene responsive to general control of amino acid biosynthesis

1987 ◽  
Vol 208 (1-2) ◽  
pp. 159-167 ◽  
Author(s):  
Kiyoji Nishiwaki ◽  
Naoyuki Hayashi ◽  
Shinji Irie ◽  
Dong-Hyo Chung ◽  
Satoshi Harashima ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Biosynthesis ◽  
General Control ◽  
Acid Biosynthesis

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.

Nitrogen regulation of amino acid catabolism in Neurospora crassa

1978 ◽  
Vol 16 (3-4) ◽  
pp. 343-354 ◽  
Author(s):  
Thomas J. Facklam ◽  
George A. Marzluf
Keyword(s):  
Amino Acid ◽  
Neurospora Crassa ◽  
Nitrogen Regulation ◽  
Amino Acid Catabolism

The Neurospora crassa cyt-20 gene encodes cytosolic and mitochondrial valyl-tRNA synthetases and may have a second function in addition to protein synthesis

1991 ◽  
Vol 11 (8) ◽  
pp. 4022-4035
Author(s):  
A R Kubelik ◽  
B Turcq ◽  
A M Lambowitz
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Neurospora Crassa ◽  
Temperature Sensitivity ◽  
Temperature Sensitive ◽  
Cellular Transport ◽  
Missense Mutations ◽  
Reading Frame ◽  
Trna Synthetases ◽  
Cytosolic Protein

The cyt-20-1 mutant of Neurospora crassa is a temperature-sensitive, cytochrome b- and aa3-deficient strain that is severely deficient in both mitochondrial and cytosolic protein synthesis (R.A. Collins, H. Bertrand, R.J. LaPolla, and A.M. Lambowitz, Mol. Gen. Genet. 177:73-84, 1979). We cloned the cyt-20+ gene by complementation of the cyt-20-1 mutation and found that it contains a 1,093-amino-acid open reading frame (ORF) that encodes both the cytosolic and mitochondrial valyl-tRNA synthetases (vaIRSs). A second mutation, un-3, which is allelic with cyt-20-1, also results in temperature-sensitive growth, but not in gross deficiencies in cytochromes b and aa3 or protein synthesis. The un-3 mutant had also been reported to have pleiotropic defects in cellular transport process, resulting in resistance to amino acid analogs (M.S. Kappy and R.L. Metzenberg, J. Bacteriol. 94:1629-1637, 1967), but this resistance phenotype is separable from the temperature sensitivity in crosses and may result from a mutation in a different gene. The 1,093-amino-acid ORF encoding vaIRSs is the site of missense mutations resulting in temperature sensitivity in both cyt-20-1 and un-3 and is required for the transformation of both mutants. The opposite strand of the cyt-20 gene encodes an overlapping ORF of 532 amino acids, which may also be functional but is not required for transformation of either mutant. The cyt-20-1 mutation in the vaIRS ORF results in severe deficiencies of both mitochondrial and cytosolic vaIRS activities, whereas the un-3 mutation does not appear to result in a deficiency of these activities or of mitochondrial or cytosolic protein synthesis sufficient to account for its temperature-sensitive growth. The phenotype of the un-3 mutant raises the possibility that the vaIRS ORF has a second function in addition to protein synthesis.

scholarly journals Amino acid deprivation induces AKT activation by inducing GCN2/ATF4/REDD1 axis

2021 ◽  
Vol 12 (12) ◽  
Author(s):  
Hyeon-Ok Jin ◽  
Sung-Eun Hong ◽  
Ji-Young Kim ◽  
Se-Kyeong Jang ◽  
In-Chul Park
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Cell Survival ◽  
Amino Acid Deprivation ◽  
General Control ◽  
Akt Activation ◽  
Amino Acid Availability ◽  
Survival Signal ◽  
Cancer Cell Survival ◽  
Glutamine Deprivation

AbstractAmino acid availability is sensed by various signaling molecules, including general control nonderepressible 2 (GCN2) and mechanistic target of rapamycin complex 1 (mTORC1). However, it is unclear how these sensors are associated with cancer cell survival under low amino acid availability. In the present study, we investigated AKT activation in non-small cell lung cancer (NSCLC) cells deprived of each one of 20 amino acids. Among the 20 amino acids, deprivation of glutamine, arginine, methionine, and lysine induced AKT activation. AKT activation was induced by GCN2/ATF4/REDD1 axis-mediated mTORC2 activation under amino acid deprivation. In CRISPR-Cas9-mediated REDD1-knockout cells, AKT activation was not induced by amino acid deprivation, indicating that REDD1 plays a major role in AKT activation under amino acid deprivation. Knockout of REDD1 sensitized cells cultured under glutamine deprivation conditions to radiotherapy. Taken together, GCN2/ATF4/REDD1 axis induced by amino acid deprivation promotes cell survival signal, which might be a potential target for cancer therapy.

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