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In vitro interaction of the carboxy‐terminal domain of lamin A with actin
Author(s) -
Sasseville A.Marie-Josée,
Langelier Yves
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00294-4
Subject(s) - lamin , nuclear lamina , chromatin , microbiology and biotechnology , inner membrane , actin , biology , domain (mathematical analysis) , chemistry , nuclear protein , biochemistry , nucleus , dna , transcription factor , gene , mitochondrion , mathematical analysis , mathematics
The nuclear lamina formed by lamins is localized between the inner nuclear membrane and chromatin. Lamins are thought to be implicated in the higher order chromatin structure. Interactions of lamins with chromatin have been described but the molecular components directly involved in these interactions remain to be identified. Using a GST‐C‐terminal domain of lamin A fusion protein to probe cellular extracts for interacting proteins, we have found that this domain of lamin A binds to nuclear actin. This result suggests that an actin‐based molecular motor linked to the lamina could be involved in the movement of chromatin domains.