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The role of the pufX protein in photosynthetic electron transfer Lilburn, Timothy George
Abstract
The role of the puJX gene product of Rhodobacter capsulatus has been unclear, but deletion of the gene renders the organism incapable of photosynthetic growth on a minimal medium. However, suppressor mutants that are able to grow photosynthetically are readily isolated. Two such suppressor mutants were characterized as to their photosynthetic growth properties, their fluorescence at five different incident light intensities, the integrity of their chromatophores and their abilities to generate a trans-membrane potential. I found that the photosynthetic apparatus in the suppressor mutants was less stable than that of the pseudo-wild type and primary mutant strain and that the suppressor mutants used light energy less efficiently than the pseudo-wild type strain. Therefore, the suppressor strains are more correctly designated partial suppressor mutants. The locations and sequences of the suppressor mutations were determined and both were found to change the second codon of the pufA gene. It is hypothesized that the serine residue encoded by this codon is important in interactions between the B870 antenna complex and other membrane-bound polypeptides. Based on these results and those of other investigators, a model for the role of the PufX protein is put forward in which the PufX protein, in conjunction with the B870 ft polypeptide, is proposed to form a gateway in the light harvesting antenna complex surrounding the reaction center. This gateway would allow the passage of quinones and quinols between the reaction center and the cytochrome blc\ complex.
Item Metadata
Title |
The role of the pufX protein in photosynthetic electron transfer
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Creator | |
Publisher |
University of British Columbia
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Date Issued |
1995
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Description |
The role of the puJX gene product of Rhodobacter capsulatus has been unclear, but
deletion of the gene renders the organism incapable of photosynthetic growth on a minimal
medium. However, suppressor mutants that are able to grow photosynthetically are readily
isolated. Two such suppressor mutants were characterized as to their photosynthetic growth
properties, their fluorescence at five different incident light intensities, the integrity of their
chromatophores and their abilities to generate a trans-membrane potential. I found that the
photosynthetic apparatus in the suppressor mutants was less stable than that of the pseudo-wild
type and primary mutant strain and that the suppressor mutants used light energy less
efficiently than the pseudo-wild type strain. Therefore, the suppressor strains are more
correctly designated partial suppressor mutants. The locations and sequences of the suppressor
mutations were determined and both were found to change the second codon of the pufA gene.
It is hypothesized that the serine residue encoded by this codon is important in interactions
between the B870 antenna complex and other membrane-bound polypeptides. Based on these
results and those of other investigators, a model for the role of the PufX protein is put forward
in which the PufX protein, in conjunction with the B870 ft polypeptide, is proposed to form a
gateway in the light harvesting antenna complex surrounding the reaction center. This gateway
would allow the passage of quinones and quinols between the reaction center and the
cytochrome blc\ complex.
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Extent |
7012355 bytes
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Genre | |
Type | |
File Format |
application/pdf
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Language |
eng
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Date Available |
2009-04-22
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Provider |
Vancouver : University of British Columbia Library
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Rights |
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.
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DOI |
10.14288/1.0088259
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URI | |
Degree | |
Program | |
Affiliation | |
Degree Grantor |
University of British Columbia
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Graduation Date |
1995-11
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Campus | |
Scholarly Level |
Graduate
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Aggregated Source Repository |
DSpace
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Item Media
Item Citations and Data
Rights
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.