Finger proteins and DNA-specific recognition: distinct patterns of conserved amino acids suggest different evolutionary modes.
Finger proteins, the first example of which was Xenopus TFIIIA, share Zn2+ 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-X2-4-C-X3-F-X5-L-X2-H-X3-H). Class II finger proteins display a single (C-X2-C-X13-C-X2-C) motif and a facultative second putative finger. The relation between the structure of finger proteins and their recognised DNA sequences is discussed.
Payre
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F
Centre de Recherche de Biochimie et Génétique Cellulaires du CNRS, Toulouse, France.
Vincent
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A
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D004247:DNA / Q000235:genetics* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D012341:RNA, Ribosomal, 5S / Q000235:genetics; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors / Q000235:genetics; D014981:Xenopus
D004268:DNA-Binding Proteins; D012341:RNA, Ribosomal, 5S; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors; D004247:DNA