Pratt L F, Cleveland D W
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
EMBO J. 1988 Apr;7(4):931-40. doi: 10.1002/j.1460-2075.1988.tb02898.x.
To characterize the alpha-tubulin gene family in chicken, we have isolated five chicken alpha-tubulin genes and determined the majority of the sequences of the encoded polypeptides. Three of these (c alpha 3, c alpha 5/6 and c alpha 8) encode novel, expressed alpha-tubulins that have not previously been analyzed, whereas one gene segment is a pseudogene and another appears capable of encoding a functional subunit (although we were unable to document its expression in a survey of chicken tissues). Together with two additional expressed, functional alpha-tubulins reported earlier, we conclude that the chicken alpha-tubulin family is comprised of at least five functional genes whose polypeptide products are substantially more heterogeneous than found in preceding analyses of vertebrate alpha-tubulins. Comparison of the amino acid sequences reveals that the five polypeptides are between 96 and 83% identical, with the extreme carboxy-terminal residues representing a highly heterogeneous variable domain. Since some alpha-tubulins undergo cyclic post-translational removal and readdition of a carboxy-terminal tyrosine, the notable sequence divergence in this domain suggests that individual tubulins probably participate to different extents in this modification cycle.
为了表征鸡的α-微管蛋白基因家族,我们分离出了五个鸡α-微管蛋白基因,并确定了所编码多肽的大部分序列。其中三个基因(cα3、cα5/6和cα8)编码新的、已表达的α-微管蛋白,这些蛋白以前未被分析过,而一个基因片段是假基因,另一个似乎能够编码一个功能亚基(尽管我们在对鸡组织的调查中未能证明其表达)。连同之前报道的另外两个已表达的功能性α-微管蛋白,我们得出结论,鸡α-微管蛋白家族由至少五个功能基因组成,其多肽产物比之前对脊椎动物α-微管蛋白的分析中发现的更加多样化。氨基酸序列比较显示,这五个多肽的同源性在96%至83%之间,极端的羧基末端残基代表一个高度异质的可变结构域。由于一些α-微管蛋白会经历羧基末端酪氨酸的循环翻译后去除和重新添加,该结构域中显著的序列差异表明,单个微管蛋白可能在这个修饰循环中参与程度不同。