Abstract：
:The Trypanosoma brucei flagellum is unusual as it is attached along the cell body and contains, in addition to an apparently conventional axoneme, a structure called the paraflagellar rod, which is essential for cell motility. Here, we investigated flagellum behaviour in normal and mutant trypanosome cell lines where expression of genes encoding various axoneme proteins (PF16, PF20, DNAI1, LC2) had been silenced by RNAi. First, we show that the propulsive wave (normally used for forward motility) is abolished in the absence of outer dynein arms, whereas the reverse wave (normally used for changing direction) still occurs. Second, in contrast to Chlamydomonas--but like metazoa, the central pair adopts a fixed orientation during flagellum beating. This orientation becomes highly variable in central-pair- and outer-dynein-arm-mutants. Third, the paraflagellar rod contributes to motility by facilitating three-dimensional wave propagation and controlling cell shape. Fourth, motility is required to complete the last stage of cell division in both insect and bloodstream stages of the parasite. Finally, our study also reveals the conservation of molecular components of the trypanosome flagellum. Coupled to the ease of reverse genetics, it raises the interest of trypanosomes as model organisms to study cilia and flagella.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Branche C,Kohl L,Toutirais G,Buisson J,Cosson J,Bastin Pdoi
10.1242/jcs.03078subject
Has Abstractpub_date
2006-08-15 00:00:00pages
3443-55issue
Pt 16eissn
0021-9533issn
1477-9137pii
jcs.03078journal_volume
119pub_type
杂志文章abstract：:There is a limited number of methods to examine transbilayer lipid distribution in biomembranes. We employed freeze-fracture replica-labelling immunoelectron microscopy in combination with lipid-binding proteins and a peptide to examine both transbilayer distribution and lateral distribution of various phospholipids i...
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abstract：:Syntaxins are thought to participate in the specific interactions between vesicles and acceptor membranes in intracellular protein trafficking. VAM3 of Saccharomyces cerevisiae encodes a 33 kDa protein (Vam3p) with a hydrophobic transmembrane segment at its C terminus. Vam3p has structural similarities to syntaxins of...
journal_title：Journal of cell science
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journal_title：Journal of cell science
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doi：
更新日期：1986-12-01 00:00:00
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doi：
更新日期：1998-01-01 00:00:00
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pub_type： 杂志文章
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journal_title：Journal of cell science
pub_type： 杂志文章
doi：
更新日期：1987-06-01 00:00:00
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journal_title：Journal of cell science
pub_type： 杂志文章
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更新日期：2008-07-15 00:00:00
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journal_title：Journal of cell science
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doi：
更新日期：1993-03-01 00:00:00
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pub_type： 杂志文章
doi：
更新日期：1992-03-01 00:00:00
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journal_title：Journal of cell science
pub_type： 杂志文章
doi：
更新日期：1990-12-01 00:00:00
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pub_type： 杂志文章
doi：
更新日期：1979-06-01 00:00:00
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journal_title：Journal of cell science
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doi：
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doi：
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doi：
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