scholarly journals DNA binding is not sufficient for nuclear localization of regulatory proteins in Saccharomyces cerevisiae.

1986 ◽  
Vol 6 (12) ◽  
pp. 4763-4766 ◽  
Author(s):  
P A Silver ◽  
R Brent ◽  
M Ptashne
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Dna Binding ◽  
Gene Product ◽  
Nuclear Localization ◽  
Binding Protein ◽  
Chimeric Protein ◽  
Dna Binding Protein ◽  
Regulatory Proteins

We showed by immunofluorescence that the procaryotic DNA-binding protein LexA and a chimeric protein that contains the DNA-binding portion of LexA (amino acids 1 to 87) and a large portion (amino acids 74 to 881) of the Saccharomyces cerevisiae positive regulatory GAL4 protein (GAL4 gene product) are not preferentially localized in the nucleus in S. cerevisiae.

DNA binding is not sufficient for nuclear localization of regulatory proteins in Saccharomyces cerevisiae

1986 ◽  
Vol 6 (12) ◽  
pp. 4763-4766
Author(s):  
P A Silver ◽  
R Brent ◽  
M Ptashne
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Dna Binding ◽  
Gene Product ◽  
Nuclear Localization ◽  
Binding Protein ◽  
Chimeric Protein ◽  
Dna Binding Protein ◽  
Regulatory Proteins

We showed by immunofluorescence that the procaryotic DNA-binding protein LexA and a chimeric protein that contains the DNA-binding portion of LexA (amino acids 1 to 87) and a large portion (amino acids 74 to 881) of the Saccharomyces cerevisiae positive regulatory GAL4 protein (GAL4 gene product) are not preferentially localized in the nucleus in S. cerevisiae.

scholarly journals Nuclear localization of the adenovirus DNA-binding protein: requirement for two signals and complementation during viral infection.

1989 ◽  
Vol 9 (10) ◽  
pp. 4372-4380 ◽  
Author(s):  
N Morin ◽  
C Delsert ◽  
D F Klessig
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Viral Infection ◽  
Nuclear Localization ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Multifunctional Protein ◽  
Nuclear Localization Signals ◽  
Amino Terminal ◽  
Amino Terminal Domain

The adenovirus DNA-binding protein (DBP) is an abundant multifunctional protein located primarily in the nuclei of infected cells. To define sequences involved in nuclear transport of DBP, a series of point and small deletion mutants were constructed via oligonucleotide-directed mutagenesis. Two short stretches of basic amino acids located in the amino-terminal domain (amino acids 42 to 46 and 84 to 89) were identified. Their importance, however, depended on the context in which DBP was expressed. Disruption of either site prevented nuclear localization after transient expression in transfected 293 cells, implying that two nuclear localization signals are necessary for transport of this nuclear protein. In contrast, the mutant DBPs synthesized during viral infection were located either primarily in the nucleus or in the nucleus and cytoplasm, depending on the mutation and the stage of the viral infection. Thus, the nuclear localization defect could be complemented by viral infection, perhaps through the interaction of the mutant polypeptide with a virus-encoded or -induced factor(s).

Nuclear localization of the adenovirus DNA-binding protein: requirement for two signals and complementation during viral infection

1989 ◽  
Vol 9 (10) ◽  
pp. 4372-4380
Author(s):  
N Morin ◽  
C Delsert ◽  
D F Klessig
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Viral Infection ◽  
Nuclear Localization ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Multifunctional Protein ◽  
Nuclear Localization Signals ◽  
Amino Terminal ◽  
Amino Terminal Domain

The adenovirus DNA-binding protein (DBP) is an abundant multifunctional protein located primarily in the nuclei of infected cells. To define sequences involved in nuclear transport of DBP, a series of point and small deletion mutants were constructed via oligonucleotide-directed mutagenesis. Two short stretches of basic amino acids located in the amino-terminal domain (amino acids 42 to 46 and 84 to 89) were identified. Their importance, however, depended on the context in which DBP was expressed. Disruption of either site prevented nuclear localization after transient expression in transfected 293 cells, implying that two nuclear localization signals are necessary for transport of this nuclear protein. In contrast, the mutant DBPs synthesized during viral infection were located either primarily in the nucleus or in the nucleus and cytoplasm, depending on the mutation and the stage of the viral infection. Thus, the nuclear localization defect could be complemented by viral infection, perhaps through the interaction of the mutant polypeptide with a virus-encoded or -induced factor(s).

scholarly journals Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae.

1992 ◽  
Vol 11 (10) ◽  
pp. 3787-3796 ◽  
Author(s):  
S. Zhang ◽  
C. Lockshin ◽  
A. Herbert ◽  
E. Winter ◽  
A. Rich
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Z Dna

scholarly journals Identity of the 17-kilodalton protein, a DNA-binding protein from Escherichia coli, and the firA gene product.

1988 ◽  
Vol 170 (12) ◽  
pp. 5916-5918 ◽  
Author(s):  
R Aasland ◽  
J Coleman ◽  
A L Holck ◽  
C L Smith ◽  
C R Raetz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Dna Binding ◽  
Gene Product ◽  
Binding Protein ◽  
Protein A ◽  
Dna Binding Protein

scholarly journals REB1, a yeast DNA-binding protein with many targets, is essential for growth and bears some resemblance to the oncogene myb.

1990 ◽  
Vol 10 (10) ◽  
pp. 5226-5234 ◽  
Author(s):  
Q D Ju ◽  
B E Morrow ◽  
J R Warner
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Rna Polymerase Ii ◽  
Essential Gene ◽  
Binding Protein ◽  
Consensus Sequence ◽  
Physiological Role ◽  
Dna Binding Protein ◽  
Reading Frame ◽  
Chromosome Ii

REB1 is a DNA-binding protein that recognizes sites within both the enhancer and the promoter of rRNA transcription as well as upstream of many genes transcribed by RNA polymerase II. We report here the cloning of the gene for REB1 by screening a yeast genomic lambda gt11 library with specific oligonucleotides containing the REB1 binding site consensus sequence. The REB1 gene was sequenced, revealing an open reading frame encoding 809 amino acids. The predicted protein was highly hydrophilic, with numerous OH-containing amino acids and glutamines, features common to many of the general DNA-binding proteins of Saccharomyces cerevisiae, such as ABF1, RAP1, GCN4, and HSF1. There was some homology between a portion of REB1 and the DNA-binding domain of the oncogene myb. REB1 is an essential gene that maps on chromosome II. However, the physiological role that it plays in the cell has yet to be established.

AND-1, a natural chimeric DNA-binding protein, combines an HMG-box with regulatory WD-repeats

1997 ◽  
Vol 110 (9) ◽  
pp. 1051-1062 ◽  
Author(s):  
A. Kohler ◽  
M.S. Schmidt-Zachmann ◽  
W.W. Franke
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Sequence Motifs ◽  
Mobility Shift ◽  
Hmg Box ◽  
Amino Terminal ◽  
Wd Repeats ◽  
Carboxy Terminal

Using a specific monoclonal antibody (mAb AND-1/23-5-14) we have identified, cDNA-cloned and characterized a novel DNA-binding protein of the clawed toad, Xenopus laevis, that is accumulated in the nucleoplasm of oocytes and various other cells. This protein comprises 1,127 amino acids, with a total molecular mass of 125 kDa and a pI of 5.27. It is encoded by a mRNA of approximately 4 kb and contains, in addition to clusters of acidic amino acids, two hallmark motifs: the amino-terminal part harbours seven consecutive ‘WD-repeats’, which are sequence motifs of about 40 amino acids that are characteristic of a large group of regulatory proteins involved in diverse cellular functions, while the carboxy terminal portion possesses a 63-amino-acid-long ‘HMG-box’, which is typical of a family of DNA-binding proteins involved in regulation of chromatin assembly, transcription and replication. The DNA-binding capability of the protein was demonstrated by DNA affinity chromatography and electrophoretic mobility shift assays using four-way junction DNA. Protein AND-1 (acidic nucleoplasmic DNA-binding protein) appears as an oligomer, probably a homodimer, and has been localized throughout the entire interchromatinic space of the interphase nucleoplasm, whereas during mitosis it is transiently dispersed over the cytoplasm. We also identified a closely related, perhaps orthologous protein in mammals. The unique features of protein AND-1, which is a ‘natural chimera’ combining properties of the WD-repeat and the HMG-box families of proteins, are discussed in relation to its possible nuclear functions.

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