Abstract
Protein-protein interactions between the nuclear lamins are responsible for the assembly of the nuclear lamina, a meshwork of intermediate filaments associated with the nuclear envelope inner membrane. We have used the yeast two-hybrid system to examine the interactions between the predominant human nuclear lamins expressed as GAL4 fusion proteins in Saccharomyces cerevisiae. Lamin A, prelamin A, lamin B1, and lamin C were able to form homodimers as well as heterodimers. Analysis of the different structural domains of lamin B1 demonstrated that the second half of coil 2 of the rod domain was necessary for the formation of the most stable homodimers. The results show that the yeast two-hybrid system can be used to study the interactions between structural proteins and their domains.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cloning, Molecular
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DNA-Binding Proteins
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Fungal Proteins / metabolism
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Humans
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Lamin Type A
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Lamin Type B*
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Lamins
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Macromolecular Substances
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Nuclear Envelope / metabolism
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Nuclear Proteins / biosynthesis
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Nuclear Proteins / metabolism*
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Plasmids
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Polymerase Chain Reaction
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Recombinant Fusion Proteins / biosynthesis
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Recombinant Fusion Proteins / metabolism*
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins*
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Transcription Factors*
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beta-Galactosidase / biosynthesis
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beta-Galactosidase / metabolism*
Substances
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DNA-Binding Proteins
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Fungal Proteins
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GAL4 protein, S cerevisiae
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Lamin Type A
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Lamin Type B
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Lamins
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Macromolecular Substances
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Nuclear Proteins
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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lamin C
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beta-Galactosidase