title: Molecular basis of sperm flagellar axonemes: structural and evolutionary aspects.
abstract: The axonemes serve as motile machineries in sperm flagella. Although atypical axonemal structures are observed in some cases, 9 + 2 microtubule structure of the axoneme is predominant in many organisms. Several structures are bound to these microtubules and comprise a highly organized protein network. Extensive proteomic analysis of the axonemes has led to find several repeats, domains, and motifs in axonemal proteins. Molecular comparison of subunit composition of axonemal substructures between the ascidian Ciona intestinalis and the green algae Chlamydomonas reinhardtti leads to an intriguing molecular aspect concerning the evolution of intracellular functional complex: The architecture of the axonemes has been well conserved through evolution, but the molecular structure of each axonemal component is not always conserved. In light of domain structure in the axonemal proteins, substructures like outer arm dynein and radial spoke contain a set of domain structures, although some domain-containing subunits are different between these two organisms. Thus, conservation of protein domains within a substructure seems to take precedence over that of each protein ("module-dominant conservation"), which may ultimately result in morphological and functional conservation of the axonemes through evolution.
authors.affiliation: Shimoda Marine Research Center, University of Tsukuba, 5-10-1 Shimoda, Shizuoka 415-0025, Japan. inaba@kurofune.shimoda.tsukuba.ac.jp
authors.forename: Kazuo
authors.initials: K
authors.lastname: Inaba
mesh_terms: D000818:Animals; D019143:Evolution, Molecular; D005407:Flagella / Q000737:chemistry* / Q000502:physiology* / Q000648:ultrastructure; D006801:Humans; D008297:Male; D008870:Microtubules / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure; D013094:Spermatozoa / Q000737:chemistry* / Q000502:physiology* / Q000648:ultrastructure