Abstract
Protein-protein interactions resulting in dimerization and heterodimerization are of central importance in the control of gene expression and cell function. Proteins that share the 52-residue LIM/double zinc-finger domain are involved in a wide range of developmental and cellular controls. Some of these functions have been hypothesized to involve protein dimerization. In the present report we demonstrate, using both in vitro and cell-based studies, that a representative LIM protein, human cysteine-rich protein (hCRP), can efficiently homodimerize. The dimerization ability of hCRP is mapped to the LIM domains, can be transferred to an unrelated protein by fusion of a single minimal LIM/double zinc-finger segment, occurs in the absence as well as the presence of DNA, and appears to depend on coordination of two zinc atoms in the finger doublet. These observations support a specific role for protein dimerization in the function of proteins containing the LIM/double zinc-finger domain and expand the general spectrum of potential interactions mediated by zinc-finger motifs.
MeSH Terms
Amino Acid Sequence
Antibodies
Cloning, Molecular
DNA-Binding Proteins/biosynthesis,chemistry,metabolism
Glutathione Transferase/biosynthesis
Humans
Macromolecular Substances
Molecular Sequence Data
Mutagenesis, Site-Directed
Nuclear Proteins
Protein Conformation
Protein Multimerization
Proteins
Proto-Oncogene Proteins c-myc/biosynthesis,chemistry,metabolism
Recombinant Fusion Proteins/biosynthesis,chemistry,metabolism
TATA Box
Transcriptional Activation
Zinc Fingers/physiology
Chemicals
Antibodies
DNA-Binding Proteins
Macromolecular Substances
Nuclear Proteins
Proteins
Proto-Oncogene Proteins c-myc
Recombinant Fusion Proteins
cysteine-rich protein, mammalian
Glutathione Transferase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Feuerstein R
Department of Genetics, University of Pennsylvania School of Medicine, Philadelphia 19104-6145.
Wang X
Song D
Cooke N E
Liebhaber S A
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