Sequence analysis of the Chlamydomonas alpha and beta dynein heavy chain genes.
Sequence analysis of the Chlamydomonas alpha and beta dynein heavy chain genes.
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发表时间：
1994-03
影响因子：
4
通讯作者：
D. Mitchell;K. Brown
中科院分区：
文献类型：
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作者：
D. Mitchell;K. Brown
我们已经测序的基因组克隆跨越完整的编码区的一个重链（β）和催化结构域的第二个（α）的莱茵衣藻鞭毛外臂动力蛋白ATP酶。β重链基因（ODA-4基因座）跨越20 kb，分为至少30个外显子，并编码预测的520 kDa蛋白质。与海胆β动力蛋白序列的比较揭示了贯穿两种蛋白质的同源性。在最保守的中心催化区，衣原体α和β链与海胆β链同样不同（分别为64%和65%相似性），而衣原体γ链与海胆β链更不同（54%相似性）。在其他动力蛋白重链中作为潜在核苷酸结合位点的四个富含甘氨酸的环也存在于衣原体α和β动力蛋白中。这四个核苷酸结合基序中的两个是高度保守的鞭毛动力蛋白，但只有基序先前确定为催化位点的海胆动力蛋白是高度保守的鞭毛和细胞质动力蛋白重链之间。二级结构的预测表明，所有的动力蛋白重链具有三个大的结构域，与四个核苷酸结合的共识序列位于中央185 kDa的域，是由形成多个，短的α-螺旋卷曲螺旋的区域的两侧有界。
We have sequenced genomic clones spanning the complete coding region of one heavy chain (beta) and the catalytic domain of a second (alpha) of the Chlamydomonas reinhardtii flagellar outer arm dynein ATPase. The beta heavy chain gene (ODA-4 locus) spans 20 kb, is divided into at least 30 exons, and encodes a predicted 520 kDa protein. Comparison with sea urchin beta dynein sequences reveals homology that extends throughout both proteins. Over the most conserved central catalytic region, the Chlamydomonas alpha and beta chains are equally divergent from the sea urchin beta chain (64% and 65% similarity, respectively), whereas the Chlamydomonas gamma chain is more divergent from urchin beta (54% similarity). The four glycine-rich loops identified as potential nucleotide-binding sites in other dynein heavy chains are also present in Chlamydomonas alpha and beta dyneins. Two of these four nucleotide-binding motifs are highly conserved among flagellar dyneins, but only the motif previously identified as the catalytic site in sea urchin dynein is highly conserved between flagellar and cytoplasmic dynein heavy chains. Predictions of secondary structure suggest that all dynein heavy chains possess three large domains, with the four nucleotide-binding consensus sequences located in a central 185 kDa domain that is bounded on both sides by regions that form multiple, short alpha-helical coiled-coils.