Biomedical subjects

T J Beanland

Publications and source records attributed to T J Beanland.

6 recordsLinked to original sources

PubMed1992

Controversy on chloroplast origins.

Controversy exists over the origins of photosynthetic organelles in that contradictory trees arise from different sequence, biochemical and ultrastructural data sets. We propose a testable hypothesis which explains this inconsistency as a result of the differing GC contents of sequences. We report that current methods of tree reconstruction tend to group sequences with similar GC contents irrespective of whether the similar GC content is due to common ancestry or is independently acquired. Nuclear encoded sequences (high GC) give different trees from chloroplast encoded sequences (low GC). We find that current data is consistent with the hypothesis of multiple origins for photosynthetic organelles and single origins for each type of light harvesting complex.

Base Composition↗

PubMed1992

Sequence of Prochloron didemni atpBE and the inference of chloroplast origins.

The prochlorophytes, oxygenic photosynthetic prokaryotes containing chlorophylls a and b, have been put forward as descended from the organisms that gave rise to chloroplasts of green plants and algae by endosymbiosis, although this has always been controversial. To assess the phylogenetic position of the prochlorophyte Prochloron didemni, we have cloned and sequenced its atpBE genes. Phylogenetic inference under a range of models gives moderate to strong support for a cyanobacterial grouping rather than a chloroplast one. Possible systematic errors in this and previous analyses of prochlorophyte sequences are discussed.

Amino Acid Sequence↗

PubMed1992

Substitutional bias confounds inference of cyanelle origins from sequence data.

Available molecular and biochemical data offer conflicting evidence for the origin of the cyanelle of Cyanophora paradoxa. We show that the similarity of cyanelle and green chloroplast sequences is probably a result of these two lineages independently developing the same pattern of directional nucleotide change (substitutional bias). This finding suggests caution should be exercised in the interpretation of nucleotide sequence analyses that appear to favor the view of a common endosymbiont for the cyanelle and chlorophyll-b-containing chloroplasts. The data and approaches needed to resolve the issue of cyanelle origins are discussed. Our findings also have general implications for phylogenetic inference under conditions where the base compositions (compositional bias) of the sequences analyzed differ.

Base Composition↗

PubMed1992

The inference of evolutionary trees from molecular data.

1. Procedures for multiple alignment of sequence data, subsequent phylogenetic inference, and testing of the trees derived are presented. 2. The assumptions underlying different approaches and the extent to which they are valid are discussed.

Amino Acid Sequence↗

PubMed1990

Evolutionary relationships between "Q-type" photosynthetic reaction centres: hypothesis-testing using parsimony.

Hypotheses concerning the evolutionary relationships between "Q-type" photosynthetic reaction centres are tested using amino acid parsimony analysis of subunit sequences and an alignment based on dot matrix comparisons. Strong evidence is found for independent gene duplications having produced the L and M subunits of the photosynthetic purple bacterial reaction centre and D1 and D2 of Photosystem-II. Much support is also found for the L and M subunits of the green filamentous bacterium Chloroflexus aurantiacus arising from the same gene duplication as the purple bacterial subunits, suggesting there was an ancestral bacterial heterodimeric reaction centre. These conclusions caution against over-extrapolation from the purple bacterial reaction centre to Photosystem-II, and suggest that the latter is more ancient than previously supposed.

Bacteria↗

PubMedDate not supplied

The ribulose bisphosphate carboxylase/oxygenase of Prochlorothrix hollandica: purification, subunit structure and partial N-terminal sequence analysis of the large subunit.

Ribulose bisphosphate carboxylase/oxygenase was purified to apparent homogeneity from the carboxysomes of Prochlorothrix hollandica. The MW of the native enzyme was estimated to be 560,000 Dalton, comprising large subunits (LSU) of 57,000 Dalton and small subunits (SSU) of 13,000, probably in an 8LSU8SSU quaternary structure. Enzyme activity was maximal at pH 8.0 at 30 degrees C. The requirement of activity for Mg2+ could not be replaced by Mn2+. Co2+, Ca2+ or Cu2+. Amino acid N-terminal sequence analysis of the LSU showed a high degree of conservation when compared to cyanobacterial and chloroplast LSU sequences but was too short to allow a reliable phylogenetic assignment of P. hollandica.

Amino Acid Sequence↗