CDNA SEQUENCING OF NUCLEAR LAMIN-A AND LAMIN-C REVEALS PRIMARY AND SECONDARY STRUCTURAL HOMOLOGY TO INTERMEDIATE FILAMENT PROTEINS
CDNA SEQUENCING OF NUCLEAR LAMIN-A AND LAMIN-C REVEALS PRIMARY AND SECONDARY STRUCTURAL HOMOLOGY TO INTERMEDIATE FILAMENT PROTEINS
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DOI：
10.1073/pnas.83.17.6450
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发表时间：
1986-09-01
影响因子：
11.1
通讯作者：
BLOBEL, G
中科院分区：
文献类型：
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作者：
FISHER, DZ;CHAUDHARY, N;BLOBEL, G
从人核纤层蛋白A和核纤层蛋白C的cDNA克隆推导的氨基酸序列显示这两种核纤层蛋白之间的同一性，除了仅存在于核纤层蛋白A中的额外的9.0-kDa羧基末端尾。核纤层蛋白A和C都含有α-约360个残基的螺旋结构域，其显示出与相应的α-螺旋杆结构域是所有中间丝蛋白的结构标志。然而，核纤层蛋白α-螺旋结构域比中间丝蛋白大14%。除了如报道的与中间丝蛋白的广泛同源性[McKeon，F.，Kirschner，M.和Caput，D.（1986）Nature（伦敦）319，463-468]，已经推导出核纤层蛋白A羧基末端的一段不同的82个氨基酸残基，并通过氨基酸测序验证。该区域含有与I型和II型表皮角蛋白的氨基和羧基末端结构域的序列同源性。核纤层蛋白A和C的组装这些和其他领域的存在的影响进行了讨论。
The amino acid sequences deduced from cDNA clones of human lamin A and lamin C show identity between these two lamins except for an extra 9.0-kDa carboxyl-terminal tail that is present only in lamin A. Both lamins A and C contain an .alpha.-helical domain of approximately 360 residues that shows striking homology to a corresponding .alpha.-helical rod domain that is the structural hallmark of all intermediate filament proteins. However, the lamin .alpha.-helical domain is 14% loarger than that of the intermediate filament proteins. In addition to the extensive homology to intermediate filament proteins as reported [McKeon, F., Kirschner, M. and Caput, D. (1986) Nature (London) 319, 463-468], a different 82-amino acid residue stretch at the carboxyl terminus of lamin A has been deduced and verified by amino acid sequencing. This region contains sequence homology to amino- and carboxyl-terminal domains of type I and type II epidermal keratins. Implications of the presence of these and other domains in lamins A and C for the assembly of the nuclear lamina are discussed.