cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins.
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% larger than that of the intermediate filament proteins. In addition to the extensive homology to intermediate filament proteins as reported [McKeon, F., Kirschner, M. & 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 carboxylterminal 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.
Fisher
D Z
DZ
Chaudhary
N
N
Blobel
G
G
D000595:Amino Acid Sequence; D000818:Animals; D002467:Cell Nucleus / Q000648:ultrastructure; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D006801:Humans; D007381:Intermediate Filament Proteins / Q000235:genetics*; D034904:Lamin Type A; D034882:Lamins; D009698:Nucleoproteins / Q000235:genetics* / Q000302:isolation & purification; D051381:Rats; D012689:Sequence Homology, Nucleic Acid
D007381:Intermediate Filament Proteins; D034904:Lamin Type A; D034882:Lamins; D009698:Nucleoproteins; C440308:lamin C; D004247:DNA