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Two intestinal specific nuclear factors binding to the lactase‐phlorizin hydrolase and sucrase‐isomaltase promoters are functionally related oligomeric molecules
Author(s) -
Troelsen J.T.,
Olsen J.,
Mitchelmore C.,
Hansen G.H.,
Sjöström H.,
Norén O.
Publication year - 1994
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 - 10.1016/0014-5793(94)80520-2
Subject(s) - lactase , sucrase , promoter , biochemistry , electrophoretic mobility shift assay , biology , nuclear protein , gene , hydrolase , microbiology and biotechnology , chemistry , transcription factor , enzyme , gene expression
Lactase‐phlorizin hydrolase (LPH) and sucrase‐isomaltase (SI) are enterocyte‐specific gene products. The identification of regulatory cis‐elements in the promoter of these two genes has enabled us to carry out comparative studies of the corresponding intestinal‐specific nuclear factors (NF‐LPH1 and SIF1‐BP). Electrophoretic mobility shift assays demonstrated that the two nuclear factors compete for binding on the same cis‐elements. The molecular size of the DNA binding polypeptide is estimated to be approximately 50 kDa for both factors. In the native form the factors are found as 250 kDa oligomeric complexes. Based on these results NF‐LPH1 and SIF1‐BP are suggested to be either identical or closely related molecules.