The DHHC domain: A new highly conserved cysteine-rich motif

The DHHC domain: A new highly conserved cysteine-rich motif
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DOI:
10.1023/a:1006932522197
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发表时间:
1999-05-01
影响因子:
4.3
通讯作者:
Gentleman, S
Gentleman, S
中科院分区:
生物学3区
文献类型:
--
作者:
Putilina, T;Wong, P;Gentleman, S

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从人类胰腺 cDNA 文库中分离出一个独特的克隆并进行测序。对推导的克隆多肽序列的检查显示出一种新形式的富含半胱氨酸的结构域,其中包括一个具有 Cys4 锌指状金属结合位点形式的区域,后面是一个复杂的 Cys-His 区域。对 Swiss-Protein 数据库的搜索在从拟南芥、线虫、酿酒酵母和粟酒裂殖酵母基因组序列推导出的 15 个开放阅读框中发现了类似的 48 个残基结构域。该结构域的高度保守性(13 个绝对保守位置和 17 个高度保守位置)表明它在细胞中具有重要功能,可能与蛋白质-蛋白质或蛋白质-DNA 相互作用有关。该克隆识别的基因位于人类 16 号染色体上,并且在脊椎动物中是保守的。 2 Kb 信息在各种人类胎儿和成人组织中表达。针对推导蛋白的肽序列制成的抗体在猴肺和视网膜亚细胞部分的免疫印迹中显示出反应性,在晚期胎儿小鼠组织和有限数量的成年小鼠组织(包括胰岛、睾丸间质细胞和视网膜丛状层)中显示出免疫组织化学反应性。
A unique clone from a human pancreatic cDNA library was isolated and sequenced. Examination of the deduced polypeptide sequence of the clone showed a new form of cysteine-rich domain that included a region with the form of a Cys4 zinc-finger-like metal binding site followed by a complex Cys-His region. Searches of the Swiss-Protein data bank found a similar 48-residue domain in fifteen open reading frames deduced from A. thaliana, C. elegans, S. cerevisiae and S. pombe genomic sequences. The high degree of conservation of this domain (13 absolutely conserved and 17 highly conserved positions) suggests that it has an important function in the cell, possibly related to protein-protein or protein-DNA interactions. The gene recognized by the clone is is localized to human chromosome 16, and is conserved in vertebrates. The 2 Kb message is expressed in various human fetal and adult tissues. An antibody made to a peptide sequence of the deduced protein showed reactivity in immunoblots of monkey lung and retinal subcellular fractions and immunohistochemically in late fetal mouse tissues and a limited number of adult mouse tissues, including pancreatic islets, Leydig cells of the testis, and the plexiform layers of the retina.