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J Biol Chem, Vol. 273, Issue 36, 22873-22876, September 4, 1998
From the Molecular Virology Section, Laboratory of Molecular
Microbiology, NIAID, National Institutes of Health,
Bethesda, Maryland 20892-0460
Activation domains of eukaryotic transcription
factors can be classified into at least three distinct types based on
their amino acid composition: acidic, proline-rich, and glutamine-rich. Acidic activators, such as yeast GAL4 and GCN4 and herpes simplex virus
VP16, have been shown to stimulate transcription in various higher and
lower eukaryotic cells. Similarly, proline-rich activators also
function in both mammalian and yeast cells. These activators are
regarded to possess "universal" activating potentials. By contrast,
several studies have suggested that glutamine-rich activators such as
human Sp1 are active in higher (mammalian) but not lower (yeast)
eukaryotic cells. One interpretation is that lower eukaryotic cells
lack a critical co-factor necessary for a glutamine-rich domain. This
reasoning is counter-intuitive because many native yeast activator
proteins contain glutamine-rich domains. Here, we have investigated the
activity of a glutamine-rich GAL4-Sp1 domain A (Sp1A) hybrid protein in
yeast Saccharomyces cerevisiae. We show that GAL4-Sp1A
activated a GAL1-lacZ reporter by more than 200-fold over
basal when the reporter was carried on a 2µ vector. The generality of
the Sp1A results is supported by our finding that yeast glutamine-rich
domains from HAP2 and MCM1 are also transcriptionally active in
S. cerevisiae. Interestingly, we found that glutamine-rich
domains are considerably less potent when responsive promoters
(i.e. GAL1-lacZ) are integrated into yeast
chromosome. Thus our results segregate the inherent transcriptional activity of a glutamine-rich domain in yeast S. cerevisiae
from its apparent lack of activity when assayed on chromosomally
embedded promoters.
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