title: Apoptotic molecular machinery: vastly increased complexity in vertebrates revealed by genome comparisons.
abstract: A comparison of the proteins encoded in the recently (nearly) completed human genome to those from the fly and nematode genomes reveals a major increase in the complexity of the apoptotic molecular machinery in vertebrates, in terms of both the number of proteins involved and their domain architecture. Several components of the apoptotic system are shared by humans and flies, to the exclusion of nematodes, which seems to support the existence of a coelomate clade in animal evolution. A considerable repertoire of apoptotic protein domains was detected in Actinomycetes and Cyanobacteria, which suggests a major contribution of horizontal gene transfer to the early evolution of apoptosis.
authors.affiliation: National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.
authors.forename: L
authors.initials: L
authors.lastname: Aravind
authors.forename: V M
authors.initials: VM
authors.lastname: Dixit
authors.forename: E V
authors.initials: EV
authors.lastname: Koonin
mesh_terms: D020816:Amino Acid Motifs; D000818:Animals; D017209:Apoptosis / Q000235:genetics; D017173:Caenorhabditis elegans / Q000235:genetics; D017124:Conserved Sequence; D004331:Drosophila melanogaster / Q000235:genetics; D019143:Evolution, Molecular; D016678:Genome; D015894:Genome, Human; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D006801:Humans; D019476:Insect Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics* / Q000502:physiology; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D013045:Species Specificity
chemical_list: D015801:Helminth Proteins; D019476:Insect Proteins; D011506:Proteins