scholarly journals UMP kinase activity is involved in proper chloroplast development in rice

2018 ◽  
Vol 137 (1) ◽  
pp. 53-67 ◽  
Author(s):  
Fei Chen ◽  
Guojun Dong ◽  
Xiaohui Ma ◽  
Fang Wang ◽  
Yanli Zhang ◽  
...  
1998 ◽  
Vol 180 (22) ◽  
pp. 5891-5895 ◽  
Author(s):  
Nevan J. Krogan ◽  
Michelle L. Zaharik ◽  
Jan Neuhard ◽  
Rod A. Kelln

ABSTRACT The dum gene of Salmonella typhimurium was originally identified as a gene involved in dUMP synthesis (C. F. Beck et al., J. Bacteriol. 129:305–316, 1977). In the genetic background used in their selection, the joint acquisition of adcd (dCTP deaminase) and a dum mutation established a condition of thymidine (deoxyuridine) auxotrophy. In this study, we show that dum is identical to pyrH, the gene encoding UMP kinase. The level of UMP kinase activity in thedum mutant was found to be only 30% of that observed for the dum + strain. Thymidine prototrophy was restored to the original dum dcd mutant (KP1361) either by transduction using a pyrH + donor or by complementation with either of twopyrH +-carrying plasmids. Thymidine auxotrophy could be reconstructed in the dum + derivative (KP1389) by the introduction of a mutant pyrH allele. To define the minimal mutational complement necessary to produce thymidine auxotrophy in thyA + strains, adcd::Km null mutation was constructed. In the wild-type background, dcd::Km alone or in combination with a pyrH (dum) mutation did not result in a thymidine requirement. A third mutation, cdd(cytidine-deoxycytidine deaminase), was required together with thedcd and pyrH mutations to impart thymidine auxotrophy.


2019 ◽  
Vol 20 (9) ◽  
pp. 2107 ◽  
Author(s):  
Qing Dong ◽  
Ying-Xin Zhang ◽  
Quan Zhou ◽  
Qun-En Liu ◽  
Dai-Bo Chen ◽  
...  

Pyrimidine nucleotides are important metabolites that are building blocks of nucleic acids, which participate in various aspects of plant development. Only a few genes involved in pyrimidine metabolism have been identified in rice and the majority of their functions remain unclear. In this study, we used a map-based cloning strategy to isolate a UMPK gene in rice, encoding the UMP kinase that phosphorylates UMP to form UDP, from a recessive mutant with pale-green leaves. In the mutant, UDP content always decreased, while UTP content fluctuated with the development of leaves. Mutation of UMPK reduced chlorophyll contents and decreased photosynthetic capacity. In the mutant, transcription of plastid-encoded RNA polymerase-dependent genes, including psaA, psbB, psbC and petB, was significantly reduced, whereas transcription of nuclear-encoded RNA polymerase-dependent genes, including rpoA, rpoB, rpoC1, and rpl23, was elevated. The expression of UMPK was significantly induced by various stresses, including cold, heat, and drought. Increased sensitivity to cold stress was observed in the mutant, based on the survival rate and malondialdehyde content. High accumulation of hydrogen peroxide was found in the mutant, which was enhanced by cold treatment. Our results indicate that the UMP kinase gene plays important roles in regulating chloroplast development and stress response in rice.


1976 ◽  
Vol 35 (03) ◽  
pp. 635-642 ◽  
Author(s):  
M Steiner

SummaryThe effect of thrombin on the phosphorylating activity of platelet membranes was compared to that of trypsin. Preincubation of non-32P phosphorylated platelet membranes with or without either of these two enzymes resulted in a considerable loss of membrane protein kinase activity which was most severe when trypsin was used. Protein kinase activity and endogenous protein acceptors decreased in parallel. 32P-phosphorylated membranes showed a slow but progressive loss of label which was accelerated by trypsin. Thrombin under these conditions prevented the loss of 32P-phosphate. These results are interpreted to indicate a thrombin-induced destruction of a phosphoprotein phosphatase. The protein kinase activity of phosphorylated platelet membranes using endogenous or exogenous protein substrates showed a significant reduction compared to non-phosphorylated membranes suggesting a deactivation of protein kinase by phosphorylation of platelet membranes. Neither thrombin nor trypsin caused a qualitative change in the membrane polypeptides accepting 32P-phosphate but resulted in quantitative alterations of their ability to become phosphorylated.


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