Carbamoyl phosphate synthetase subunit Cpa1 interacting with Dut1, controls development, arginine biosynthesis, and pathogenicity of Colletotrichum gloeosporioides

2020 ◽  
Author(s):  
Qingqun Tan ◽  
Xuanzhu Zhao ◽  
Haiyong He ◽  
Junxiang Zhang ◽  
Tuyong Yi
Keyword(s):  
Colletotrichum Gloeosporioides ◽  
Carbamoyl Phosphate Synthetase ◽  
Arginine Biosynthesis ◽  
Carbamoyl Phosphate

scholarly journals The Pyrimidine Operon pyrRPB-carA fromLactococcus lactis

2001 ◽  
Vol 183 (9) ◽  
pp. 2785-2794 ◽  
Author(s):  
Jan Martinussen ◽  
Jette Schallert ◽  
Birgit Andersen ◽  
Karin Hammer
Keyword(s):  
Mutational Analysis ◽  
Regulatory Gene ◽  
Regulatory Protein ◽  
Small Subunit ◽  
Transcriptional Level ◽  
Carbamoyl Phosphate Synthetase ◽  
Arginine Biosynthesis ◽  
Carbamoyl Phosphate ◽  
Biosynthetic Genes ◽  
Membrane Bound

ABSTRACT The four genes pyrR, pyrP, pyrB, and carAwere found to constitute an operon in Lactococcus lactissubsp. lactis MG1363. The functions of the different genes were established by mutational analysis. The first gene in the operon is the pyrimidine regulatory gene, pyrR, which is responsible for the regulation of the expression of the pyrimidine biosynthetic genes leading to UMP formation. The second gene encodes a membrane-bound high-affinity uracil permease, required for utilization of exogenous uracil. The last two genes in the operon, pyrBand carA, encode pyrimidine biosynthetic enzymes; aspartate transcarbamoylase (pyrB) is the second enzyme in the pathway, whereas carbamoyl-phosphate synthetase subunit A (carA) is the small subunit of a heterodimeric enzyme, catalyzing the formation of carbamoyl phosphate. The carAgene product is shown to be required for both pyrimidine and arginine biosynthesis. The expression of the pyrimidine biosynthetic genes including the pyrRPB-carA operon is subject to control at the transcriptional level, most probably by an attenuator mechanism in which PyrR acts as the regulatory protein.

Arginine synthesis by hepatomas in vitro. I. The requirements for cell growth in medium containing ornithine in place of arginine and the isolation and characterization of variant hepatomas auxotrophic for arginine

1984 ◽  
Vol 68 (1) ◽  
pp. 285-303 ◽  
Author(s):  
S.J. Goss
Keyword(s):  
Cell Growth ◽  
The Other ◽  
Gene Products ◽  
Carbamoyl Phosphate Synthetase ◽  
Arginine Biosynthesis ◽  
Carbamoyl Phosphate ◽  
Isolation And Characterization ◽  
Ornithine Transcarbamoylase

Cell growth in ‘ornithine-medium’ requires the expression of two liver-specific genes, those for ornithine transcarbamoylase (OTC) and carbamoyl phosphate synthetase I (CPS-I). CPS-II appears unable to replace CPS-I in this system. The need for N-acetylglutamate (to activate CPS-I) can be met, at least in part, by providing it in the medium. The other gene products involved in arginine biosynthesis are probably all ubiquitous (i.e. not tissue-specific). In an attempt to study the factors responsible for the expression of liver-specific genes, variant hepatomas are isolated that have lost the ability to grow in ornithine-medium. Two classes of ‘orn-’ variants are identified: unstable variants that require dexamethasone for adequate CPS-I production, and ‘stable’ variants that have lost many liver-specific traits. Studies on one stable variant show that it can revert (though rarely), and that it regains its various liver-specific traits in a non-coordinate fashion.

scholarly journals In Lactobacillus plantarum, Carbamoyl Phosphate Is Synthesized by Two Carbamoyl-Phosphate Synthetases (CPS): Carbon Dioxide Differentiates the Arginine-Repressed from the Pyrimidine-Regulated CPS

2000 ◽  
Vol 182 (12) ◽  
pp. 3416-3422 ◽  
Author(s):  
Hervé Nicoloff ◽  
Jean-Claude Hubert ◽  
Françoise Bringel
Keyword(s):  
Carbon Dioxide ◽  
Lactic Acid ◽  
Lactic Acid Bacterium ◽  
Lactobacillus Plantarum ◽  
Bicarbonate Level ◽  
Carbamoyl Phosphate Synthetase ◽  
Wild Type ◽  
Arginine Biosynthesis ◽  
Carbamoyl Phosphate ◽  
Double Deletion

ABSTRACT Carbamoyl phosphate (CP) is an intermediate in pyrimidine and arginine biosynthesis. Carbamoyl-phosphate synthetase (CPS) contains a small amidotransferase subunit (GLN) that hydrolyzes glutamine and transfers ammonia to the large synthetase subunit (SYN), where CP biosynthesis occurs in the presence of ATP and CO2.Lactobacillus plantarum, a lactic acid bacterium, harbors a pyrimidine-inhibited CPS (CPS-P; Elagöz et al., Gene 182:37–43, 1996) and an arginine-repressed CPS (CPS-A). Sequencing has shown that CPS-A is encoded by carA (GLN) and carB (SYN). Transcriptional studies have demonstrated that carB is transcribed both monocistronically and in the carABarginine-repressed operon. CP biosynthesis in L. plantarumwas studied with three mutants (ΔCPS-P, ΔCPS-A, and double deletion). In the absence of both CPSs, auxotrophy for pyrimidines and arginine was observed. CPS-P produced enough CP for both pathways. In CO2-enriched air but not in ordinary air, CPS-A provided CP only for arginine biosynthesis. Therefore, the uracil sensitivity observed in prototrophic wild-type L. plantarum without CO2 enrichment may be due to the low affinity of CPS-A for its substrate CO2 or to regulation of the CP pool by the cellular CO2/bicarbonate level.

scholarly journals Analysis of the rrl3 Mutants Reveals the Importance of Arginine Biosynthesis in the Maintenance of Root Apical Meristem in Rice

2017 ◽  
Vol 7 (1) ◽  
pp. 36
Author(s):  
Israt J. Shelley ◽  
Sayaka Watanabe ◽  
Hiroaki Ozaki ◽  
Nobuhiro Nagasawa ◽  
Atsushi Ogawa ◽  
...  
Keyword(s):  
Apical Meristem ◽  
Culture Medium ◽  
Root Apical Meristem ◽  
Root Tip ◽  
Quiescent Center ◽  
Carbamoyl Phosphate Synthetase ◽  
Arginine Biosynthesis ◽  
Carbamoyl Phosphate ◽  
Short Root ◽  
Spatiotemporal Expression

We characterized reduced root length3(rrl3) mutantsof rice that exhibit a short-root phenotype under conditions producing mechanical impediments to growth, such as aerated water culture medium. The mutants were not able to maintain the quiescent center (QC) identity and produced disorganized root apical meristem (RAM) under aeration because of impaired cell division. A map-based cloning approach showed that RRL3 encodes carbamoyl phosphate synthetase (CPS) which is thought to be required for the conversion of ornithine into citrulline during arginine biosynthesis. The RRL3 gene is expressed highly at the root tip area that includes the root cap and division zone. The RRL3 gene expression level was greatly affected by aeration treatment, indicating that the spatiotemporal expression of the RRL3 gene with respect to the aeration is important for the maintenance of RAM. Furthermore, the application of citrulline and arginine could rescue the root phenotype, which implied that arginine biosynthesis was impaired in the rrl3-1 mutant. These results suggest that the RRL3 regulated arginine biosynthesis is important for the maintenance of RAM organization in the presence of mechanical impediments. 

scholarly journals Product inhibition studies on bovine liver carbamoyl phosphate synthetase

1974 ◽  
Vol 141 (3) ◽  
pp. 817-824 ◽  
Author(s):  
Keith R. F. Elliott ◽  
Keith F. Tipton
Keyword(s):  
Inorganic Phosphate ◽  
Substrate Binding ◽  
Inorganic Ions ◽  
Bovine Liver ◽  
Product Inhibition ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Product Release ◽  
Proposed Model ◽  
Inhibition Studies

A study of the product-inhibition patterns of carbamoyl phosphate synthetase from bovine liver is reported. Inhibition by adenosine, AMP and inorganic ions is also reported. The results are in agreement with the previously proposed model in which the order of substrate binding is ATPMg, followed by HCO3−, ATPMg and NH4+. The order of product release on the basis of the reported results is carbamoyl phosphate, followed by ADPMg, ADPMg and inorganic phosphate.

Inactivation by acivicin of carbamoyl-phosphate synthetase II of human colon carcinoma

1985 ◽  
Vol 34 (1) ◽  
pp. 97-100 ◽  
Author(s):  
Judith S. Sebolt ◽  
Takashi Aoki ◽  
John N. Eble ◽  
John L Glover ◽  
George Weber
Keyword(s):  
Colon Carcinoma ◽  
Human Colon ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Human Colon Carcinoma

Spatial relationships among the active and allosteric sites of carbamoyl-phosphate synthetase

1985 ◽  
Vol 13 (2) ◽  
pp. 98-109 ◽  
Author(s):  
Philip G. Kasprzyk ◽  
Eric Whalen-Pederson ◽  
Paul M. Anderson ◽  
Joseph J. Villafranca
Keyword(s):  
Spatial Relationships ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Allosteric Sites
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