TY - JOUR
T1 - Functional domains of the transcriptional activator NUC-1 in Neurospora crassa
AU - Kang, Seogchan
N1 - Funding Information:
I would like to thank the former and presentm embers of the lab with whom I havet ruly enjoyedw orking.I am indebtedt o M.A. Nelson,J . Grotelueschena,n d D. Butler for their stimulatingd iscussionsA. bove all, I am deeply gratefult o my mentorP rofessorR .L. Metzenbergfo r his support,a dvice,a nd encouragemenTt.h is researchw as supported by U.S. Public Health Service Grant GM 08995t o R.L. Metzenberg.
PY - 1993/8/25
Y1 - 1993/8/25
N2 - The NUC-1 regulatory protein directly controls the transcription of genes encoding the phosphorus acquisition enzymes in Neurospora crassa. To understand how NUC-1 regulates the transcription of these genes and how the activity of NUC-1 is modulated by other regulatory proteins, two putative functional domains of NUC-1 were analyzed: the DNA-binding domain and the regulatory domain. The DNA-binding activity of NUC-1 has not been directly demonstrated; however, results of deletion analysis, sequence analysis of the nuc-1 mutant alleles, and strong sequence similarity with the Saccharomyces cerevisiae PHO4 protein strongly suggest that the basic helix-loop-helix motif of NUC-1 forms a DNA-binding domain. Deletion and mutant analyses revealed that 39 amino acid (aa) residues (aa 463 to 501), or fewer, of NUC-1 are interacting with the negative regulatory factor(s), the PREG and/or PGOV proteins.
AB - The NUC-1 regulatory protein directly controls the transcription of genes encoding the phosphorus acquisition enzymes in Neurospora crassa. To understand how NUC-1 regulates the transcription of these genes and how the activity of NUC-1 is modulated by other regulatory proteins, two putative functional domains of NUC-1 were analyzed: the DNA-binding domain and the regulatory domain. The DNA-binding activity of NUC-1 has not been directly demonstrated; however, results of deletion analysis, sequence analysis of the nuc-1 mutant alleles, and strong sequence similarity with the Saccharomyces cerevisiae PHO4 protein strongly suggest that the basic helix-loop-helix motif of NUC-1 forms a DNA-binding domain. Deletion and mutant analyses revealed that 39 amino acid (aa) residues (aa 463 to 501), or fewer, of NUC-1 are interacting with the negative regulatory factor(s), the PREG and/or PGOV proteins.
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U2 - 10.1016/0378-1119(93)90428-6
DO - 10.1016/0378-1119(93)90428-6
M3 - Article
C2 - 8359693
AN - SCOPUS:0027219676
SN - 0378-1119
VL - 130
SP - 259
EP - 264
JO - Gene
JF - Gene
IS - 2
ER -