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Genetic and physical characterization of putP, the proline carrier gene of Escherichia coli K12 (1986)

Mogi, Tatsushi ; Yamamoto, Hiroshi ; Nakao, Toshifumi ; [et al.]

Springer

Molecular genetics and genomics 202 (1986), S. 35-41

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ISSN: 1617-4623

Keywords: Proline carrier gene ; putP ; Escherichia coli ; putC ; proT

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary Two new mutants of E. coli K12, strains PT9 and PT32 were isolated, that were defective in proline transport. They had no high affinity proline transport activity, but their cytoplasmic membranes retained proline binding activity with altered sensitivity to inhibition by p-chloromercuribenzoate(pCMB). The lesion was mapped at the putP gene, which is located at min 23 on the revised E. coli genetic map (Bachmann 1983) as a composite gene in the proline utilization gene cluster, putP, putC, and putA, arranged in this order. The putC gene was shown to regulate the synthesis of proline dehydrogenase (putA gene product). Hybrid plasmids carrying the put region (Motojima et al. 1979; Wood et al. 1979) were used to construct the physical map of the put region. The possible location of the putP gene in the DNA segment was determined by subcloning the putP gene, genetic complementation, and recombination analyses using several proline transport mutants.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00330513

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Resonance raman study on axial ligands of heme irons in cytochrome bd-type ubiquinol oxidase from Escherichia coli (1995)

Hirota, Shun ; Mogi, Tatsushi ; Anraku, Yasuhiro ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Biospectroscopy 1 (1995), S. 305-311

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ISSN: 1075-4261

Keywords: Chemistry ; Analytical Chemistry and Spectroscopy

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Physics

Notes: Resonance Raman (RR) spectra of cytochrome bd-type ubiquinol oxidase enriched with Fe-isotopes were investigated with excitation at 406.7, 424.0, 427.0, 441.6, and 647.1 nm. The bands of reduced form at 252 and 400 cm-1 were tentatively assigned to vFe—His of high-spin b595 and vFe—Met of low-spin b558, respectively. The vFe—O2 and δFeOO bands of heme d-O2 were observed at 566 and ∼445 cm-1, respectively. The vFe—CO frequency of heme d-CO was unusually low (477 cm-1) but the v4 frequency was not of P-450 type. Therefore, the axial ligand of heme d would not be an ordinary histidine or cysteine. © 1995 John Wiley & Sons, Inc.

Additional Material: 3 Ill.