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Purification of a NF1‐like DNA‐binding protein from rat liver and cloning of the corresponding cDNA.
Author(s) -
Paonessa G.,
Gounari F.,
Frank R.,
Cortese R.
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb03178.x
Subject(s) - biology , molecular cloning , complementary dna , cloning (programming) , gene , microbiology and biotechnology , computational biology , genetics , computer science , programming language
NF1‐like proteins play a role in transcription of liver‐specific genes. A DNA‐binding protein, recognizing half of the canonical NF1 binding site (TGGCA) present on the human albumin and retinol‐binding protein genes, has been purified from rat liver. Several peptides deriving from a tryptic digest of the purified protein were sequenced and the sequence was used to synthesize specific oligonucleotides. Two overlapping cDNA clones were obtained from a rat‐liver cDNA library; their sequence reveals an open reading frame coding for 505 amino acids, including all the peptides sequenced from the purified protein. The DNA‐binding domain, most likely located within the first 250 amino acids, is highly homologous to the sequence of CTF/NF1 purified from HeLa cells. Northern analysis reveals several mRNA species present in different combinations in various rat tissues.