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Finger proteins and DNA‐specific recognition: Distinct patterns of conserved amino acids suggest different evolutionary modes
Author(s) -
Payre François,
Vincent Alain
Publication year - 1988
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(88)80091-7
Subject(s) - amino acid , dna , conserved sequence , biology , genetics , computational biology , evolutionary biology , chemistry , base sequence
Finger proteins, the first example of which was Xenopus TFIIIA, share Zn 2+ finger‐like folded domains capable of binding to nucleic acids. A large number of this type of protein have been characterised from diverse organisms, indicating a wide evolutionary spread of the DNA‐binding fingers. At least two classes of finger proteins may be distinguished. Class I proteins contain variable numbers of the tandemly repeating TFIIIA‐like finger motif, (Y/F‐X‐C‐X 2–4 ‐C‐X 3 ‐F‐X 5 ‐L‐X 2 ‐H‐X 3 ‐H). Class II finger proteins display a single (C‐X 2 ‐C‐X 13 ‐C‐X 2 ‐C) motif and a facultative second putative finger. The relation between the structure of finger proteins and their recognised DNA sequences is discussed.