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Sequence variation in transcription factor IIIA.

C J Gaskins¹, J S Hanas

¹Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City 73190.

Nucleic Acids Research

|April 25, 1990

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Investigating transcription factor IIIA (TFIIIA) in Xenopus and Rana species reveals significant sequence variation, particularly in the C-terminal region, impacting transcription promotion. This highlights differential evolution rates of TFIIIA domains.

Area of Science:

Molecular Biology
Developmental Biology
Genetics

Background:

Previous research identified macromolecular differences between Xenopus and Rana transcription factor IIIA (TFIIIA).
TFIIIA plays a crucial role in gene transcription.
Understanding TFIIIA's structure and function is key to deciphering gene regulation.

Purpose of the Study:

To clone and sequence cDNAs for TFIIIA from Xenopus borealis and Rana catesbeiana.
To gain molecular insight into the structure, function, and species variation of TFIIIA and its zinc finger domains.
To analyze sequence conservation and divergence across different TFIIIA proteins.

Main Methods:

Cloning and sequencing of TFIIIA cDNAs from Xenopus borealis and Rana catesbeiana.
Amino acid sequence comparison and homology analysis with Xenopus laevis TFIIIA.

Related Experiment Videos

Hydropathy analysis to predict protein structure and functional regions.

Main Results:

Xenopus borealis and Rana catesbeiana TFIIIAs exhibit significant sequence variation compared to Xenopus laevis TFIIIA (84% and 63% homology, respectively).
Sequence variation is non-random, with greater divergence in the C-terminal (transcription promotion) regions than the N-terminal (DNA contact) regions.
Hydropathy analyses reveal conserved zinc finger periodicity in N-terminal regions and extreme hydrophilicity in C-terminal regions, with distinct C-terminal hydropathy in Rana catesbeiana TFIIIA.

Conclusions:

TFIIIA exhibits substantial species-specific sequence variation, particularly in functionally distinct domains.
The N-terminal DNA-binding region is highly conserved, while the C-terminal transcription-promoting region is more divergent.
TFIIIA zinc fingers are less conserved than other protein domains, suggesting differential evolutionary rates and adaptation.