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Specific Domain of cGMP‐Dependent Protein Kinase Iβ but Not Iα Functions as a Transcriptional Activator in Yeast
Author(s) -
Yuasa Keizo,
Omori Kenji,
Yanaka Noriyuki
Publication year - 2000
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/713803583
Subject(s) - leucine zipper , activator (genetics) , microbiology and biotechnology , biology , amino acid , transcription factor , transcription (linguistics) , protein kinase a , protein kinase c , transcriptional regulation , biochemistry , kinase , gene , linguistics , philosophy
Recently, cyclic GMP‐dependent protein kinase (cGK) was shown to translocate to the nucleus and regulate gene transcription. To determine whether cGK I proteins function as transcriptional activators, we produced the constructs of cGK Ialpha or Ibeta fused with the DNA binding domain of the yeast transcriptional activator GAL4. Here, we demonstrate that the amino‐terminal region of cGK Ibeta (amino acids 1‐107) exhibits transcriptional activation in yeast. However, full‐length cGK Ialpha and Ibeta and the amino‐terminal region of cGKIalpha had no transcriptional activation function. Amino acid replacement in the leucine zipper motif of the amino‐terminal region of cGK Ibeta substantially reduced transcriptional activation. These results suggest that the Ibeta‐specific region in cGK I proteins may interact with other proteins by way of the leucine zipper motif and has a transcriptional activation function.