The protein Id: A negative regulator of helix-loop-helix DNA binding proteins

Cell ◽  
1990 ◽  
Vol 61 (1) ◽  
pp. 49-59 ◽  
Author(s):  
Robert Benezra ◽  
Robert L. Davis ◽  
Daniel Lockshon ◽  
David L. Turner ◽  
Harold Weintraub
1990 ◽  
Vol 599 (1 Cell Lineages) ◽  
pp. 1-11 ◽  
Author(s):  
ROBERT BENEZRA ◽  
ROBERT L. DAVIS ◽  
ANDREW LASSAR ◽  
STEPHEN TAPSCOTT ◽  
MATHEW THAYER ◽  
...  

1991 ◽  
Vol 11 (2) ◽  
pp. 1156-1160
Author(s):  
C Murre ◽  
A Voronova ◽  
D Baltimore

Recent studies have identified a family of DNA-binding proteins that share a common DNA-binding and dimerization domain with the potential to form a helix-loop-helix (HLH) structure. Various HLH proteins can form heterodimers that bind to a common DNA sequence, termed the E2-box. We demonstrate here that E2-box-binding B-cell- and myocyte-specific nuclear factors contain subunits which are identical or closely related to ubiquitously expressed (E12/E47) HLH proteins. These biochemical function for E12/E47-like molecules in mammalian differentiation, similar to the genetically defined function of daughterless in Drosophila development.


1990 ◽  
Vol 10 (11) ◽  
pp. 5927-5936
Author(s):  
H Wang ◽  
I Clark ◽  
P R Nicholson ◽  
I Herskowitz ◽  
D J Stillman

The SIN3 gene (also known as SDI1) is a negative regulator of the yeast HO gene. Mutations in SIN3 suppress the requirement for the SWI5 activator for expression of the yeast HO gene and change the normal asymmetric pattern of HO expression in mother and daughter cells. Furthermore, the in vitro DNA-binding activity of several DNA-binding proteins is reduced in extracts prepared from sin3 mutants. We have cloned the SIN3 gene and determined that a haploid strain with a SIN3 gene disruption is viable. We determined the sequence of the SIN3 gene, which is predicted to encode a 175-kDa polypeptide with four paired amphipathic helix motifs. These motifs have been identified in the myc family of helix-loop-helix DNA-binding proteins and in the TPR family of regulatory proteins. The SIN3 transcript was mapped, and it was determined that the SIN3 transcript was absent in stationary-phase cells. Immunofluorescence microscopy with anti-SIN3 antibody demonstrated that SIN3 protein was present in nuclei. A comparison of restriction map and sequence data revealed that SIN3 is the same as regulatory genes UME4 and RPD1.


1991 ◽  
Vol 11 (2) ◽  
pp. 1156-1160 ◽  
Author(s):  
C Murre ◽  
A Voronova ◽  
D Baltimore

Recent studies have identified a family of DNA-binding proteins that share a common DNA-binding and dimerization domain with the potential to form a helix-loop-helix (HLH) structure. Various HLH proteins can form heterodimers that bind to a common DNA sequence, termed the E2-box. We demonstrate here that E2-box-binding B-cell- and myocyte-specific nuclear factors contain subunits which are identical or closely related to ubiquitously expressed (E12/E47) HLH proteins. These biochemical function for E12/E47-like molecules in mammalian differentiation, similar to the genetically defined function of daughterless in Drosophila development.


1990 ◽  
Vol 10 (11) ◽  
pp. 5927-5936 ◽  
Author(s):  
H Wang ◽  
I Clark ◽  
P R Nicholson ◽  
I Herskowitz ◽  
D J Stillman

The SIN3 gene (also known as SDI1) is a negative regulator of the yeast HO gene. Mutations in SIN3 suppress the requirement for the SWI5 activator for expression of the yeast HO gene and change the normal asymmetric pattern of HO expression in mother and daughter cells. Furthermore, the in vitro DNA-binding activity of several DNA-binding proteins is reduced in extracts prepared from sin3 mutants. We have cloned the SIN3 gene and determined that a haploid strain with a SIN3 gene disruption is viable. We determined the sequence of the SIN3 gene, which is predicted to encode a 175-kDa polypeptide with four paired amphipathic helix motifs. These motifs have been identified in the myc family of helix-loop-helix DNA-binding proteins and in the TPR family of regulatory proteins. The SIN3 transcript was mapped, and it was determined that the SIN3 transcript was absent in stationary-phase cells. Immunofluorescence microscopy with anti-SIN3 antibody demonstrated that SIN3 protein was present in nuclei. A comparison of restriction map and sequence data revealed that SIN3 is the same as regulatory genes UME4 and RPD1.


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