Medical Journals

Molecular Basis of Sperm Flagellar Axonemes: Structural and Evolutionary Aspects.

Authors:
  • Inaba Kazuo

From: Shimoda Marine Research Center, University of Tsukuba, 5-10-1 Shimoda, Shizuoka 415-0025, Japan. inaba@kurofune.shimoda.tsukuba.ac.jp

Annals of the New York Academy of Sciences

  • Publish Date: Apr 2007
  • ISSN: 0077-8923
  • Volume: 1101
  • Issue:
  • Pages: 506-26
  • Medium: Print
  • Language: English
  • Citation (JAMA): Inaba Kazuo, et al. Molecular Basis of Sperm Flagellar Axonemes: Structural and Evolutionary Aspects.. Ann. N. Y. Acad. Sci. Apr 2007;1101:506-26

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.

Mesh Headings (Keywords): Animals, Evolution, Molecular, Flagella, Humans, Male, Microtubules, Spermatozoa


Check for Full Text / PubMed Unique Identifier (PMID): 17363437


This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.

Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.

The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.


Advertisements

About | Privacy Policy | Business Solutions | Advertise | Contact | Add Healia to your site

©2012. Healia / Meredith Corporation  

Use of this site constitutes acceptance of our Terms of Service and Privacy Policy. All content on this Web site, including medical opinion and any other health-related information, is for informational purposes only and should not be used for a specific diagnosis or individual treatment plan for any situation. Use of this site and the information contained herein does not create a doctor-patient relationship. Always seek the direct advice of your doctor in connection with any questions or issues you may have regarding your own health or the health of others.