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The predicted molecular structure suggests that CTF/NF‐I may function as a histone acetylase
Author(s) -
Oikarinen Jouko,
Mannermaa Riitta-Maaria
Publication year - 1990
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(90)81039-q
Subject(s) - histone , structure function , transcription factor , biology , dna replication , dna , microbiology and biotechnology , gene , chemistry , genetics , physics , particle physics
The primary structure of nuclear factor‐I (CTF/NF‐I), a eukaryotic regulatory DNA‐binding protein involved in both DNA replication and gene transcription, and the secondary structure predictable from it, are compared here with those of a number of prokaryotic acetylases. Hydropathy and Chou‐Fasman analyses reveal that the polypeptide chain of CTF/NF‐I is likely to fold to higher order structures similar to those of the acetylases, and significant conservation of functionally important regions of the acetylases is observed in CTF/NF‐I. It is therefore suggested that CTF/NF‐I may function as a histone acetylase.