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Biomedical subjects

Louise E Anderson

Publications and source records attributed to Louise E Anderson.

4 recordsLinked to original sources

Enzyme co-localization in pea leaf chloroplasts: glyceraldehyde-3-P dehydrogenase, triose-P isomerase, aldolase and sedoheptulose bisphosphatase.

Nearest neighbor analysis of immunocytolocalization experiments indicates that the enzymes glyceraldehyde-3-P dehydrogenase, triose-P isomerase and aldolase are located close to one another in the pea leaf chloroplast stroma, and that aldolase is located close to sedoheptulose bisphosphatase. Direct transfer of the triose phosphates between glyceraldehyde-3-P dehydrogenase and triose-P isomerase, and from glyceraldehyde-3-P dehydrogenase and triose-P isomerase to aldolase, is then a possibility, as is direct transfer of sedoheptulose bisphosphate from aldolase to sedoheptulose bisphosphatase. Spatial organization of these enzymes may be important for efficient CO(2) fixation in photosynthetic organisms. In contrast, there is no indication that fructose bisphosphatase is co-localized with aldolase, and direct transfer of fructose bisphosphate from aldolase to fructose bisphosphatase seems unlikely.

Chloroplasts↗

Mass Spectrometric Evidence for an Alternate Disulfide Bond in Chloroplast Fructose Bisphosphatase.

Mass mapping analysis based on cyanylation (CN) of the protein and CN-induced cleavage indicates that all three cysteine residues in the insertion into the light-activated pea leaf chloroplast fructose bisphosphatase (E.C. 3.1.3.11) are able to participate in disulfide bond formation. There is a major peak in the mass spectrum of the cleavage products indicating that Cys173 forms a disulfide bond with Cys153, consistent with the structure of the oxidized enzyme in PDB files 1d9q and 1dcu, and a minor peak indicating that Cys173 forms an alternate disulfide bond with Cys178. The Cys173-Cys178 disulfide bond was not apparent in the available crystal structures.

CN-induced cleavage↗

Enzyme co-localization with rubisco in pea leaf chloroplasts.

Immunocytolocalization experiments indicate that carbonic anhydrase, phosphoribulokinase, and P-glycerate kinase are near neighbors of Rubisco in the pea leaf chloroplast stroma. Direct transfer of ribulose bisphosphate and gaseous CO(2) from phosphoribulokinase and carbonic anhydrase to Rubisco, and direct transfer of P-glycerate from Rubisco to P-glycerate kinase in the chloroplast stroma, is then a possibility. Rubisco activase, responsible for the removal of inhibitory sugar phosphates that bind to the active site of Rubisco in the dark, also appears to be co-localized with Rubisco.

Journal Article↗

A quantitative method for assessing co-localization in immunolabeled thin section electron micrographs.

A method is introduced for the analysis of nearest neighbor distances between immunogold particles marking proteins on electron micrographs. Deviation from the distribution that is predicted by chance indicates co-localization of the labeled species, and the potential for productive interaction in vivo. Application of this method to the analysis of nearest neighbor distances in experiments with pea leaf thin sections and isozyme-directed antibodies indicates that glyceraldehyde-3-P dehydrogenase is located near P-glycerate kinase and near aldolase in the chloroplast stroma, consistent with the notion that these enzymes are part of a multi-enzyme photosynthetic CO(2)-fixation complex in situ.

Cell Compartmentation↗