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Fig. 5. The alterations D205N and A208T are close to (D205N) and within (A208T) helix 6 of {alpha}-tubulin. The Chlamydomonas amino acid sequence of {alpha}-tubulin (red) and ß-tubulin (white) was modeled onto the bovine tubulin crystal structure. (A) Amino acid changes observed in tua2 alleles (eight blue) and in one revertant allele (blue). (B) Part of the predicted structure, showing helix 6 with A208 and the nearby D205 with respect to the adjacent helix 5 (with P173). (C) The increased length of the side chain in the P173L alteration in revertant tua2-3R1 has probably major effects on the structure of {alpha}-tubulin. P173 is conserved in most tubulins.





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