Analysis of striated fiber formation by recombinant SF-assemblin in vitro

Journal of Molecular Biology
K F Lechtreck

Abstract

The basal bodies of green flagellates are often connected to striated microtubule-associated fibers (SMAFs), which are highly ordered bundles of 2 nm filaments. SF-assemblin (33 kDa) is the principal structural subunit of the SMAFs and consists of a non-helical head domain of approximately 32 residues and an alpha-helical rod domain that shows a pronounced coiled-coil forming ability. To investigate the functional role of the head domain we expressed N-terminally truncated molecules using a cDNA coding for SF-assemblin from Chlamydomonas reinhardtii. Recombinant wild-type SF-assemblin or molecules with an N-terminal deletion of ten residues formed striated fibers with an axial repeat of 28 nm. N-terminal truncations of 19 and 29 residues yielded assembly-incompetent molecules, revealing that the head domain is necessary for the constitution of striated fibers. Further, molecules with an internal deletion of 24 residues or with duplicated segments corresponding to insertions of 29 and 58 residues were constructed. The resulting fibers had altered cross-striation patterns and axial repeats. The observed shifts in the axial repeat corresponded well to the number of inserted or deleted residues, indicating a linear coherence betwee...Continue Reading

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Citations

Dec 19, 1998·Cell Motility and the Cytoskeleton·K F Lechtreck, M Melkonian
Jul 19, 2018·Cells·Jenna Lynne Wingfield, Karl-Ferdinand Lechtreck
Jan 5, 2014·Nature Reviews. Microbiology·Maria E Francia, Boris Striepen
Feb 12, 2010·Bioinorganic Chemistry and Applications·Shiguo ChenDongfeng Wang
Jun 18, 2002·Journal of Structural Biology·Matthew R HicksDerek N Woolfson
Apr 23, 2003·Molecular and Biochemical Parasitology·Karl-Ferdinand Lechtreck
Aug 19, 2021·Journal of Cell Science·Robert Mahen

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