Access the full text.
Sign up today, get DeepDyve free for 14 days.
K. Kashiwagi, A. Kuraishi, H. Tomitori, A. Igarashi, K. Nishimura, A. Shirahata, K. Igarashi (2000)
Identification of the Putrescine Recognition Site on Polyamine Transport Protein PotE*The Journal of Biological Chemistry, 275
D. Molenaar, J. Bosscher, B. Brink, A. Driessen, W. Konings (1993)
Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneriJournal of Bacteriology, 175
O. Lowry, N. Rosebrough, A. Farr, R. Randall (1951)
Protein measurement with the Folin phenol reagent.The Journal of biological chemistry, 193 1
(1996)
Energy transduction by ion currents
Seymour Cohen (1998)
A Guide to the Polyamines
Ned Watson, D. Dunyak, E. Rosey, J. Slonczewski, Eric OLSONlt (1992)
Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pHJournal of Bacteriology, 174
G. Kimmich, J. Randles, J. Brand (1975)
Assay of picomole amounts of ATP, ADP, and AMP using the luciferase enzyme system.Analytical biochemistry, 69 1
K. Kashiwagi, S. Miyamoto, F. Suzuki, H. Kobayashi, K. Igarashi (1992)
Excretion of putrescine by the putrescine-ornithine antiporter encoded by the potE gene of Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America, 89
Tabor Tabor, Tabor Tabor (1984)
PolyaminesAnnu Rev Biochem, 53
J. Lolkema, B. Poolman, W. Konings (1998)
Bacterial solute uptake and efflux systems.Current opinion in microbiology, 1 2
H. Houng, A. Lynn, B. Rosen (1986)
ATP-driven calcium transport in membrane vesicles of Streptococcus sanguisJournal of Bacteriology, 168
H. Tomitori, Keiko Kashiwagi, Tomoko Asakawa, Y. Kakinuma, Anthony Michael, K. Igarashi (2001)
Multiple polyamine transport systems on the vacuolar membrane in yeast.The Biochemical journal, 353 Pt 3
K. Igarashi, K. Kashiwagi, Hidehisa Hamasaki, Atsuko Miura, Tomohito, Kakegawa, Seiyu Hirose, Shigeru Matsuzaki (1986)
Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyaminesJournal of Bacteriology, 166
Keiko Kashiwagi, K. Igarashi (1988)
Adjustment of polyamine contents in Escherichia coliJournal of Bacteriology, 170
S. Cunningham-Rundles, W. Maas (1975)
Isolation, characterization, and mapping of Escherichia coli mutants blocked in the synthesis of ornithine decarboxylaseJournal of Bacteriology, 124
Melody Neely, Eric Olson (1996)
Kinetics of expression of the Escherichia coli cad operon as a function of pH and lysineJournal of Bacteriology, 178
T. Kakegawa, K. Takamiya, T. Ogawa, Y. Hayashi, S. Hirose, M. Niitsu, K. Samejima, K. Igarashi (1988)
Effect of various polyamine analogs on in vitro polypeptide synthesis.Archives of biochemistry and biophysics, 261 2
Madoka Yoshida, D. Meksuriyen, K. Kashiwagi, G. Kawai, K. Igarashi (1999)
Polyamine Stimulation of the Synthesis of Oligopeptide-binding Protein (OppA)The Journal of Biological Chemistry, 274
K. Kashiwagi, Sanae Shibuya, H. Tomitori, A. Kuraishi, K. Igarashi (1997)
Excretion and Uptake of Putrescine by the PotE Protein in Escherichia coli*The Journal of Biological Chemistry, 272
Keietsu Abe, F. Ohnishi, K. Yagi, T. Nakajima, T. Higuchi, M. Sano, M. Machida, Rafiquel Sarker, P. Maloney (2002)
Plasmid-Encoded asp Operon Confers a Proton Motive Metabolic Cycle Catalyzed by an Aspartate-Alanine Exchange ReactionJournal of Bacteriology, 184
Madoka Yoshida, K. Kashiwagi, G. Kawai, A. Ishihama, K. Igarashi (2001)
Polyamine Enhancement of the Synthesis of Adenylate Cyclase at the Translational Level and the Consequential Stimulation of the Synthesis of the RNA Polymerase ς28 Subunit*The Journal of Biological Chemistry, 276
T. Ubbink‐Kok, B. Poolman, W. Konings (1995)
Characterization of the proton/glutamate symport protein of Bacillus subtilis and its functional expression in Escherichia coliJournal of Bacteriology, 177
Yoshida Yoshida, Meksuriyen Meksuriyen, Kashiwagi Kashiwagi, Kawai Kawai, Igarashi Igarashi (1999)
Polyamine stimulation of the synthesis of oligopeptide‐binding protein (OppA). Involvement of a structural change of the Shine‐Dalgarno sequence and the initiation codon AUG in OppA mRNAJ Biol Chem, 274
K. Kashiwagi, R. Watanabe, K. Igarashi (1994)
Involvement of ribonuclease III in the enhancement of expression of the speF-potE operon encoding inducible ornithine decarboxylase and polyamine transport protein.Biochemical and biophysical research communications, 200 1
Miho Takayama, T. Ohyama, Kazuel Igarashi, Hiroshi Kobayashi (1994)
Escherichia coli cad operon functions as a supplier of carbon dioxideMolecular Microbiology, 11
K. Kashiwagi, Yuki Yamaguchi, Y. Sakai, Hiroshi Kobayashi, K. Igarashi (1990)
Identification of the polyamine-induced protein as a periplasmic oligopeptide binding protein.The Journal of biological chemistry, 265 15
H. Tomitori, K. Kashiwagi, K. Sakata, Y. Kakinuma, K. Igarashi (1999)
Identification of a Gene for a Polyamine Transport Protein in Yeast*The Journal of Biological Chemistry, 274
V. Anantharam, M. Allison, P. Maloney (1989)
Oxalate:formate exchange. The basis for energy coupling in Oxalobacter.The Journal of biological chemistry, 264 13
Milton Salton, Hubert Lechevalier (1971)
Bacterial membranes.CRC critical reviews in microbiology, 1 1
S. Meng, G. Bennett (1992)
Nucleotide sequence of the Escherichia coli cad operon: a system for neutralization of low extracellular pHJournal of Bacteriology, 174
J. Sambrook, David Russell (2006)
Dot and slot hybridization of purified RNA.CSH protocols, 2006 1
K. Igarashi, Keiko Kashiwagi (1999)
Polyamine transport in bacteria and yeast.The Biochemical journal, 344 Pt 3
(2001)
Appendix 3: vectors and bacterial strains
S. Andersson, A. Zomorodipour, Jan Andersson, Thomas Sicheritz-Pontén, U. Alsmark, R. Podowski, A. Näslund, A. Eriksson, H. Winkler, Charles Kurland (1998)
The genome sequence of Rickettsia prowazekii and the origin of mitochondriaNature, 396
H. Kaback (1971)
[13] Bacterial MembranesMethods in Enzymology, 22
Sagl Needle, Asd Christus, D. Wuksch
A General Method Applicable to the Search for Similarities in the Amino Acid Sequence of Two Proteins
K. Igarashi, K. Kashiwagi (2000)
Polyamines: mysterious modulators of cellular functions.Biochemical and biophysical research communications, 271 3
Madoka Yoshida, K. Kashiwagi, G. Kawai, A. Ishihama, K. Igarashi (2002)
Polyamines Enhance Synthesis of the RNA Polymerase ς38 Subunit by Suppression of an Amber Termination Codon in the Open Reading Frame*The Journal of Biological Chemistry, 277
Y. Kohara, K. Akiyama, K. Isono (1987)
The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic libraryCell, 50
K. Kashiwagi, T. Suzuki, F. Suzuki, T. Furuchi, H. Kobayashi, K. Igarashi (1991)
Coexistence of the genes for putrescine transport protein and ornithine decarboxylase at 16 min on Escherichia coli chromosome.The Journal of biological chemistry, 266 31
J. Belasco (1990)
The ompA 5' untranslated RNA segment functions in Escherichia coli as a growth-rate-regulated mRNA stabilizer whose activity is unrelated to translational efficiencyJournal of Bacteriology, 172
K. Igarashi, Kumiko Sugawara, I. Izumi, Chieko Nagayama, Seiyu Hirose (1974)
Effect of polyamines of polyphenylalanine synthesis by Escherichia coli and rat-liver ribosomes.European journal of biochemistry, 48 2
Summary The functions of the putative cadaverine transport protein CadB were studied in Escherichia coli. CadB had both cadaverine uptake activity, dependent on proton motive force, and cadaverine excretion activity, acting as a cadaverine‐lysine antiporter. The Km values for uptake and excretion of cadaverine were 20.8 and 303 µM respectively. Both cadaverine uptake and cadaverine‐lysine antiporter activities of CadB were functional in cells. Cell growth of a polyamine‐requiring mutant was stimulated slightly at neutral pH by the cadaverine uptake activity and greatly at acidic pH by the cadaverine‐lysine antiporter activity. At acidic pH, the operon containing cadB and cadA, encoding lysine decarboxylase, was induced in the presence of lysine. This caused neutralization of the extracellular medium and made possible the production of CO2 and cadaverine and aminopropylcadaverine instead of putrescine and spermidine. The induction of the cadBA operon also generated a proton motive force. When the cadBA operon was not induced, the expression of the speF–potE operon, encoding inducible ornithine decarboxylase and a putrescine‐ornithine antiporter, was increased. The results indicate that the cadBA operon plays important roles in cellular regulation at acidic pH.
Molecular Microbiology – Wiley
Published: Mar 1, 2004
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.