Faculty Opinions recommendation of The Saccharomyces cerevisiae helicase Rrm3p facilitates replication past nonhistone protein-DNA complexes.

2004 ◽  
Author(s):  
Frederick R Cross
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Complexes ◽  
Nonhistone Protein

scholarly journals The Saccharomyces cerevisiae Helicase Rrm3p Facilitates Replication Past Nonhistone Protein-DNA Complexes

2003 ◽  
Vol 12 (6) ◽  
pp. 1525-1536 ◽  
Author(s):  
Andreas S. Ivessa ◽  
Brian A. Lenzmeier ◽  
Jessica B. Bessler ◽  
Lara K. Goudsouzian ◽  
Sandra L. Schnakenberg ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Complexes ◽  
Nonhistone Protein

scholarly journals Immunospecificity of chromatin nonhistone protein-DNA complexes in normal and neoplastic growth

FEBS Letters ◽  
1974 ◽  
Vol 42 (1) ◽  
pp. 94-97 ◽  
Author(s):  
Jen Fu Chiu ◽  
Catherine Craddock ◽  
H. Morris ◽  
L.S. Hnilica
Keyword(s):  
Dna Complexes ◽  
Neoplastic Growth ◽  
Nonhistone Protein

Gamma-Radiation-Induced Crosslinking of Cell-Specific Chromosomal Nonhistone Protein-DNA Complexes in HeLa Chromatin

1981 ◽  
Vol 86 (1) ◽  
pp. 102 ◽  
Author(s):  
Ryszard Olinski ◽  
Robert C. Briggs ◽  
Lubomir S. Hnilica ◽  
Janet Stein ◽  
Gary Stein
Keyword(s):  
Gamma Radiation ◽  
Dna Complexes ◽  
Nonhistone Protein ◽  
Radiation Induced

scholarly journals Interaction between Nonhistone Protein HMGB1 and Linker Histone H1 Facilitates the Formation of Structurally Ordered DNA-Protein Complexes

2012 ◽  
Vol 27 ◽  
pp. 393-398 ◽  
Author(s):  
Alexander Polyanichko ◽  
Elena Chikhirzhina
Keyword(s):  
Protein Complexes ◽  
Histone H1 ◽  
Linker Histone ◽  
Chromosomal Protein ◽  
Dna Complexes ◽  
Force Microscopy ◽  
Linker Histone H1 ◽  
Nonhistone Protein ◽  
Atomic Force ◽  
Nonhistone Chromosomal Protein

The structural organization of the DNA complexes with nonhistone chromosomal protein and linker histone H1 was studied using circular dichroism spectroscopy (CD) and atomic force microscopy (AFM). It has been shown that due to the interaction between HMGB1 and H1 highly ordered DNA-protein complexes emerge in the solution. Their spectral properties are found to be similar to those of DNA/HMGB1-(AB) complexes, reported earlier. AFM images reveal the formation of fibril-like structures in the solution. We suggest that the electrostatic screening of the HMGB1 C-terminal domain by histone H1 facilitates stronger interaction of the HMGB1/H1 with DNA and the formation of the ordered supramolecular DNA-protein complexes.

scholarly journals Testing for DNA Tracking by MOT1, a SNF2/SWI2 Protein Family Member

1999 ◽  
Vol 19 (1) ◽  
pp. 412-423 ◽  
Author(s):  
David T. Auble ◽  
Susanne M. Steggerda
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Transcription Factor ◽  
Family Member ◽  
Binding Sites ◽  
Atp Hydrolysis ◽  
Tata Binding Protein ◽  
Protein Family ◽  
Dna Complexes ◽  
Dna Templates ◽  
Dependent Interaction

ABSTRACT Proteins in the SNF2/SWI2 family use ATP hydrolysis to catalyze rearrangements in diverse protein-DNA complexes. How ATP hydrolysis is coupled to these rearrangements is unknown, however. One attractive model is that these ATPases are ATP-dependent DNA-tracking enzymes. This idea was tested for the SNF2/SWI2 protein family member MOT1. MOT1 is an essential Saccharomyces cerevisiae transcription factor that uses ATP to dissociate TATA binding protein (TBP) from DNA. By using a series of DNA templates with one or two TATA boxes in combination with binding sites for heterologous DNA binding “roadblock” proteins, the ability of MOT1 to track along DNA was assayed. The results demonstrate that, following ATP-dependent TBP-DNA dissociation, MOT1 dissociates rapidly from the DNA by a mechanism that does not require a DNA end. Template commitment footprinting experiments support the conclusion that ATP-dependent DNA tracking by MOT1 does not occur. These results support a model in which MOT1 drives TBP-DNA dissociation by a mechanism that involves a transient, ATP-dependent interaction with TBP-DNA which does not involve ATP-dependent DNA tracking.

scholarly journals Cdc48 regulates intranuclear quality control sequestration of the Hsh155 splicing factor in budding yeast

2020 ◽  
Vol 133 (23) ◽  
pp. jcs252551 ◽  
Author(s):  
Veena Mathew ◽  
Arun Kumar ◽  
Yangyang K. Jiang ◽  
Kyra West ◽  
Annie S. Tam ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Quality Control ◽  
Essential Role ◽  
Protein Quality ◽  
Budding Yeast ◽  
Protein Quality Control ◽  
Genotoxic Stress ◽  
Splicing Factor ◽  
Dna Complexes ◽  
Partner Proteins

ABSTRACTCdc48 (known as VCP in mammals) is a highly conserved ATPase chaperone that plays an essential role in the assembly and disassembly of protein–DNA complexes and in degradation of misfolded proteins. We find that in Saccharomyces cerevisiae budding yeast, Cdc48 accumulates during cellular stress at intranuclear protein quality control sites (INQ). We show that Cdc48 function is required to suppress INQ formation under non-stress conditions and to promote recovery following genotoxic stress. Cdc48 physically associates with the INQ substrate and splicing factor Hsh155, and regulates its assembly with partner proteins. Accordingly, cdc48 mutants have defects in splicing and show spontaneous distribution of Hsh155 to INQ aggregates, where it is stabilized. Overall, this study shows that Cdc48 regulates deposition of proteins at INQ and suggests a previously unknown role for Cdc48 in the regulation or stabilization of splicing subcomplexes.This article has an associated First Person interview with the first author of the paper.

scholarly journals Identification and analysis of a functional human homolog of the SPT4 gene of Saccharomyces cerevisiae.

1996 ◽  
Vol 16 (6) ◽  
pp. 2848-2856 ◽  
Author(s):  
G A Hartzog ◽  
M A Basrai ◽  
S L Ricupero-Hovasse ◽  
P Hieter ◽  
F Winston
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nuclear Protein ◽  
Human Gene ◽  
Chromosome 17 ◽  
Pcr Analysis ◽  
Somatic Cell Hybrid Panel ◽  
Related Gene ◽  
Nonhistone Protein ◽  
Human Chromosome 17 ◽  
Mutant Phenotypes

Spt4p is a nonhistone protein of Saccharomyces cerevisiae that is believed to be required for normal chromatin structure and transcription. In this work we describe the isolation and analysis of a human gene, SUPT4H, that encodes a predicted protein 42% identical to Spt4p. When expressed in S. cerevisiae, SUPT4H complemented all spt4 mutant phenotypes. In human cells SUPT4H encodes a nuclear protein that is expressed in all tissues tested. In addition, hybridization analyses suggest that an SUPT4H-related gene is also present in mice. SUPT4H was localized to human chromosome 17 by PCR analysis of a human-rodent somatic cell hybrid panel. Thus, like other proteins that are components of or control the structure of chromatin, Spt4p appears to be conserved from S. cerevisiae to mammals.

Torus Circumference and Thickness Parameters From a Linear DNA Size Series Suggest How Toruses Self-Assemble

1985 ◽  
Vol 43 ◽  
pp. 522-523
Author(s):  
George C. Ruben ◽  
Kenneth A. Marx
Keyword(s):  
Tertiary Structure ◽  
Dna Complexes ◽  
Tertiary Structures ◽  
Self Assembling ◽  
Double Stranded Dna ◽  
Calf Thymus ◽  
Dna Organization ◽  
Condensed Dna ◽  
Dna Size

Certain double stranded DNA bacteriophage and viruses are thought to have their DNA organized into large torus shaped structures. Morphologically, these poorly understood biological DNA tertiary structures resemble spermidine-condensed DNA complexes formed in vitro in the total absence of other macromolecules normally synthesized by the pathogens for the purpose of their own DNA packaging. Therefore, we have studied the tertiary structure of these self-assembling torus shaped spermidine- DNA complexes in a series of reports. Using freeze-etch, low Pt-C metal (10-15Å) replicas, we have visualized the microscopic DNA organization of both calf Thymus( CT) and linear 0X-174 RFII DNA toruses. In these structures DNA is circumferentially wound, continuously, around the torus into a semi-crystalline, hexagonal packed array of parallel DNA helix sections.

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