Cloning, sequencing, and expression of a gene encoding the monomeric isocitrate dehydrogenase of the nitrogen-fixing bacterium, Azotobacter vinelandii.
作者： Takehiko SAHARA , Yasuhiro TAKADA , Yoji TAKEUCHI , Naoto YAMAOKA , Noriyuki FUKUNAGA
DOI: 10.1271/BBB.66.489
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摘要: Isocitrate dehydrogenase (IDH: EC 1.1.1.42) of Azotobacter vinelandii was purified to an electrophoretically homogeneous state, and a gene (icd) encoding this enzyme cloned sequenced. The N-terminal amino acid sequence the consistent with that deduced from nucleotide icd gene. showed high identity (62–66%) those other bacterial monomeric IDHs. Expression in Escherichia coli examined by measuring activity mRNA level. Primer extension analyses revealed two species mRNAs different lengths 5′-untranslated regions (TS-1 TS-2) were present, which 5′-terminals TS-2 sites) cytosines located at 244 bp 101 upstream translational initiation codon, respectively. Conserved promoter elements present —35 —10 TS-1 site, whereas no such common motif found region site. De...
sci-hub.se 参考文章(27)
M.G. YATES, Biochemistry of Nitrogen Fixation Amino Acids and Derivatives#R##N#A Comprehensive Treatise. pp. 1- 64 ,(1980) , 10.1016/B978-0-12-675405-6.50007-3
E. A. Mudd, P. Prentki, D. Belin, H. M. Krisch, Processing of unstable bacteriophage T4 gene 32 mRNAs into a stable species requires Escherichia coli ribonuclease E The EMBO Journal. ,vol. 7, pp. 3601- 3607 ,(1988) , 10.1002/J.1460-2075.1988.TB03238.X
Stanley G. Knight, P. W. Wilson, Experiments in bacterial physiology Burgess. ,(1949)
A M Patel, S D Dunn, Degradation of Escherichia coli uncB mRNA by multiple endonucleolytic cleavages. Journal of Bacteriology. ,vol. 177, pp. 3917- 3922 ,(1995) , 10.1128/JB.177.14.3917-3922.1995
Frederick C. Neidhardt, Philip L. Bloch, David F. Smith, Culture Medium for Enterobacteria Journal of Bacteriology. ,vol. 119, pp. 736- 747 ,(1974) , 10.1128/JB.119.3.736-747.1974
Noriyuki Fukunaga, Sigeki Imagawa, Takehiko Sahara, Atsushi Ishii, Masahiro Suzuki, Purification and characterization of monomeric isocitrate dehydrogenase with NADP(+)-specificity from Vibrio parahaemolyticus Y-4. Journal of Biochemistry. ,vol. 112, pp. 849- 855 ,(1992) , 10.1093/OXFORDJOURNALS.JBCHEM.A123988
Atsushi ISHII, Toshiro OCHIAI, Shigeki IMAGAWA, Noriyuki FUKUNAGA, Shoji SASAKI, Osamu MINOWA, Yusuke MIZUNO, Hiroyuki SHIOKAWA, Isozymes of isocitrate dehydrogenase from an obligately psychrophilic bacterium, Vibrio sp. strain ABE-1: purification, and modulation of activities by growth conditions. Journal of Biochemistry. ,vol. 102, pp. 1489- 1498 ,(1987) , 10.1093/OXFORDJOURNALS.JBCHEM.A122196
M Suzuki, T Sahara, J Tsuruha, Y Takada, N Fukunaga, Differential expression in Escherichia coli of the Vibrio sp. strain ABE-1 icdI and icdII genes encoding structurally different isocitrate dehydrogenase isozymes. Journal of Bacteriology. ,vol. 177, pp. 2138- 2142 ,(1995) , 10.1128/JB.177.8.2138-2142.1995
J. H. Hurley, P. E. Thorsness, V. Ramalingam, N. H. Helmers, D. E. Koshland, R. M. Stroud, Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 86, pp. 8635- 8639 ,(1989) , 10.1073/PNAS.86.22.8635
Mark L. LEYLAND, David J. KELLY, Purification and characterization of a monomeric isocitrate dehydrogenase with dual coenzyme specificity from the photosynthetic bacterium Rhodomicrobium vannielii FEBS Journal. ,vol. 202, pp. 85- 93 ,(1991) , 10.1111/J.1432-1033.1991.TB16347.X