Journal: Applied and Environmental Microbiology

Article Title: Genetic Complementation of an Outer Membrane Cytochrome omcB Mutant of Shewanella putrefaciens MR-1 Requires omcB Plus Downstream DNA

doi: 10.1128/aem.68.6.2781-2793.2002

Figure Lengend Snippet: FIG. 2. Linear orientation of the gene cluster of MR-1 from omcA downstream, as derived from the preliminary genomic sequence data provided by The Institute for Genomic Research (http://www.tigr.org). The diagram is drawn to scale, and the transcription direction for all genes is from left to right (5 3 3). The relative positions of some of the ORFs and complementing fragments are indicated at the bottom; position 1 corresponded to the first base of the start codon of omcA. The solid boxes below the gene cluster indicate the DNA fragments used in complementation studies. omcA and omcB encode OM cytochromes involved in Mn(IV) reduction (32, 34), while mtrA and mtrB have putative roles in metal reduction (2, 3). Other possible ORFs (orf1 through orf9 and altA) with some sequence homology to known genes from other species are also shown. The best matches to these ORFs, as identified by BLAST analysis, are shown in Table 3.

Article Snippet: The separation and purity of these subcellular fractions were assessed by spectral cytochrome content analysis (21), membrane buoyant density analysis (21), and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) with gels (15, 19) stained for protein with Pro-Blue (Owl Separation Systems, Woburn, Mass.)

Techniques: Derivative Assay, Sequencing

Journal: Applied and Environmental Microbiology

Article Title: Genetic Complementation of an Outer Membrane Cytochrome omcB Mutant of Shewanella putrefaciens MR-1 Requires omcB Plus Downstream DNA

doi: 10.1128/aem.68.6.2781-2793.2002

Figure Lengend Snippet: FIG. 5. Specific cytochrome contents of the subcellular fractions prepared from strains MR-1 and OMCB1 that were grown anaerobi- cally with fumarate as the electron acceptor. The strains contained various plasmids derived from either pVK100 (A) or pJQ200KS (B). The specific cytochrome content is the difference between the absor- bance at the peak and the absorbance at the trough of the Soret region for reduced-minus-oxidized difference spectra per milligram of pro- tein. The values are means standard deviations based on the results of independent experiments (n 3 independent cultures of each strain). The section signs, number sign, and double daggers indicate that values are statistically significantly different from the values for MR-1/pVK100 (A) and MR-1/pJQ200KS (B) at P 0.001, P 0.01, and P 0.05, respectively. Note the different y-axis scales for panels A and B.

Article Snippet: The separation and purity of these subcellular fractions were assessed by spectral cytochrome content analysis (21), membrane buoyant density analysis (21), and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) with gels (15, 19) stained for protein with Pro-Blue (Owl Separation Systems, Woburn, Mass.)

Techniques: Derivative Assay

Journal: Applied and Environmental Microbiology

Article Title: Genetic Complementation of an Outer Membrane Cytochrome omcB Mutant of Shewanella putrefaciens MR-1 Requires omcB Plus Downstream DNA

doi: 10.1128/aem.68.6.2781-2793.2002

Figure Lengend Snippet: FIG. 12. Specific cytochrome contents of the subcellular fractions prepared from strains MR-1/pVK100 and ALTA1 that were grown anaerobically with fumarate as the electron acceptor. The specific cytochrome content is the difference between the absorbance at the peak and the absorbance at the trough of the Soret region from reduced-minus-oxidized difference spectra per milligram of protein. The values are means standard deviations based on results of inde- pendent experiments (n 3 independent cultures of each strain). The differences between the two strains were not statistically significant (P 0.05).

Article Snippet: The separation and purity of these subcellular fractions were assessed by spectral cytochrome content analysis (21), membrane buoyant density analysis (21), and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) with gels (15, 19) stained for protein with Pro-Blue (Owl Separation Systems, Woburn, Mass.)

Techniques: