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Nucleic Acids Research, 1994, Vol. 22, No. 19 3983-3989
© 1994

MOLECULAR BIOLOGY

Plant activating sequences: positively charged peptides are functional as transcriptional activation domains

Juan J. Estruch*, Lyle Crossland and Stephen A. Goff

CIBA Agricultural Biotechnology Research Triangle Park, NC 27709-2257, USA

*To whom correspondence should be addressed

Received May 3, 1994. Revised August 5, 1994. Accepted August 5, 1994.

Plant sequences that act as transcriptional activation domains in yeast as well as in plants have been isolated by genetic selection in yeast. The selection was based on the reconstitution of a functional GAL4 transcriptional activator. Since the peptides show no homology with reported activation domains, they represent a new class of activating sequences. The sequence P1, which is 10 amino acids long, is the shortest functional activation domain reported. A cDNA that encodes the P14 class (peptides P14–P18) activating sequence have been cloned. The protein exhibits strong homology (higher than 50% amino acid identity) with the BBC1-related sequences, a highly conserved family of basic proteins containing nuclear localization signals. The P14 and P15 peptides are the most effective plant activating sequences. The P14 and P15 peptides are highly hydrophilic, positively charged and mostly unstructured. These properties are at odds with the ones usually found in known activation domains.


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