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A more recent version of this article appeared on May 1, 2003
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Submitted on August 22, 2002
Revised on January 8, 2003
Accepted on January 8, 2003
1 School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, Manchester, M13 9PT England UK (present address: Department of Biological Sciences Federal University of Technology, Bosso Road, P.M.B 65, Minna, Nigeria)
2 School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, Manchester, M13 9PT England UK (present address: Laboratoire de Parasitologie Molelulaire, UMR-CNRS 5016, Université Bordeaux 2, 146 rue Léo Saignat, 33076, Bordeaux Cedex, France)
3 School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, Manchester, M13 9PT England UK (present address: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE)
* Corresponding author. E-mail address: keith.gull{at}pathology.ox.ac.uk.
In trypanosomes the large mitochondrial genome within the kinetoplast is physically connected to the flagella basal bodies and is segregated by them during cell growth. The structural linkage enabling these phenomena is unknown. We have developed novel extraction / fixation protocols in order to characterize the links involved in kinetoplast-flagellum attachment and segregation. We show that three specific components comprise a structure that we have termed the Tripartite Attachment Complex (TAC). The TAC involves a set of filaments linking the basal bodies to a zone of differentiated outer and inner mitochondrial membranes and a further set of intramitochondrial filaments linking the inner face of the differentiated membrane zone to the kinetoplast. The TAC and flagellum-kDNA connections are sustained throughout the cell cycle and are replicated and remodeled during the periodic kDNA S phase. This understanding of the high order trans-membrane linkage provides an explanation for the spatial position of the trypanosome mitochondrial genome and its mechanism of segregation. Moreover, the architecture of the TAC suggests that it may also function in providing a structural and vectorial role during replication of this catenated mass of mitochondrial DNA. We suggest that this complex may represent an extreme form of a more generally occurring mitochondrion/cytoskeleton interaction.
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