tailieunhanh - Báo cáo Y học: The evolution of monomeric and oligomeric bc-type crystallins

The case of homologous monomeric c-type and oligomeric b-type crystallins has been described and analyzed in evolutionary terms. Data and hypotheses from molecular genetics and structural investigations converge and suggest a novel three-phase model for the evolutionary history of crystallin-type proteins. In the divergent cascades of monomeric and oligomeric crystallins, a pivotal role was played by alterations in the gene segments encoding the C-terminal extensions and the intermotif or interdomain linker peptides. These were genomic hot spots where evolution experimented to produce the modern variety of bc-crystallin-type quaternary structures. Keywords: crystallins; evolution; quaternary structure; introns late; introns early. . | Eur. J. Biochem. 269 3122-3130 2002 FEBS 2002 doi REVIEW ARTICLE The evolution of monomeric and oligomeric Pc-type crystallins Facts and hypotheses Giuseppe D Alessio Dipartimento di Chimica Biologica Universita di Napoli Federico II Naples Italy The case of homologous monomeric y-type and oligomeric b-type crystallins has been described and analyzed in evolutionary terms. Data and hypotheees from molecular genetics and structural investigations converge and suggest a novel three-phase model for the evolutionary history of crystallin-type proteins. In the diveggent cacc-ades of monomeric and oligomeric crystallins a pivotal role was played by alterations in the gene segments encoding the C-terminal extensions and the intermotif or interdomain linker peptides. These were genomic hot spots where evolution experimented to produce the modern variety of by-crystallin-type quaternary structures. Keywords crystallins evolution quaternary structure introns late introns early. The question of how oligomeric proteins evolved has gained renewed interest in the last few years 1-9 . AlthoLlth the possibility cannot be excluded that some proteins emerged first as functional aggregates and later dissociated into functional monomers the available evidence suggests that divergent evolution more often used the association of protein protomers into oligomers to vary and enrich the cell repertoire of structures and functions. T idrnre for frns evolutionary path can be seen in the hydrophilic effect recorded at intersubunit interfaces 3 . a surprising significant presence of polar and charged residues at oligomeric can be readily interpreted as the result of the association of previously exposed hydrophilic surfaces from a monomer into solvent-excluded interfaces in an oligomer . It has been argued that the alteration of a protein surface to render it adhesive for the generation of oligomers would be too long an evolutionary process .

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