Richard R. Burgess

ORCID: 0000-0001-9545-3165
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Research Areas
  • RNA and protein synthesis mechanisms
  • Bacterial Genetics and Biotechnology
  • Bacteriophages and microbial interactions
  • DNA and Nucleic Acid Chemistry
  • Protein purification and stability
  • Monoclonal and Polyclonal Antibodies Research
  • RNA Research and Splicing
  • RNA modifications and cancer
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Viral Infectious Diseases and Gene Expression in Insects
  • Molecular Biology Techniques and Applications
  • Enzyme-mediated dye degradation
  • DNA Repair Mechanisms
  • Diffusion and Search Dynamics
  • Genomics and Chromatin Dynamics
  • Advanced biosensing and bioanalysis techniques
  • Low-power high-performance VLSI design
  • Plant tissue culture and regeneration
  • Microbial Metabolic Engineering and Bioproduction
  • Genomics and Phylogenetic Studies
  • Transgenic Plants and Applications
  • Glycosylation and Glycoproteins Research
  • Cancer therapeutics and mechanisms
  • Fungal and yeast genetics research

University of Wisconsin–Madison
2011-2024

University of Alabama in Huntsville
2023

Center for Cancer Research
2005

Philips (Netherlands)
1990-2002

Biotechnology Institute
1990-1995

Oklahoma State University
1995

University of Virginia
1995

Philips (Finland)
1994

Biotechnology Research Center
1994

University of Wisconsin System
1993-1994

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTProcedure for the rapid, large-scale purification of Escherichia coli DNA-dependent RNA polymerase involving polymin P precipitation and DNA-cellulose chromatographyRichard R. Burgess Jerome J. JendrisakCite this: Biochemistry 1975, 14, 21, 4634–4638Publication Date (Print):October 1, 1975Publication History Published online1 May 2002Published inissue 1 October...

10.1021/bi00692a011 article EN Biochemistry 1975-10-01

This paper describes a method for the puritication of Escherichia coli DNA-dependent RNA polymerase which is rapid, reproducible, high in yield, and able to handle preparations using from 1 g 3 kg cells.The involves disruption bacterial cells with glass beads Waring Blendor, digestion DNase I, centrifugation remove ribosomes debris, fractionation ammonium sulfate, chromatography on diethylaminoethyl cellulose, phosphocellulose, Bio-Gel A-1Sm.Addition 5% glycerol 0.1 mu dithiothreitol all...

10.1016/s0021-9258(18)63520-3 article EN cc-by Journal of Biological Chemistry 1969-11-01

A backbone model of a 10-subunit yeast RNA polymerase II has been derived from x-ray diffraction data extending to 3 angstroms resolution. All 10 subunits exhibit high degree identity with the corresponding human proteins, and 9 are conserved among three eukaryotic polymerases I, II, III. Notable features include pair jaws, formed by Rpb1, Rpb5, Rpb9, that appear grip DNA downstream active center. clamp on nearer center, Rpb2, Rpb6, may be locked in closed position RNA, accounting for great...

10.1126/science.288.5466.640 article EN Science 2000-04-28

Abstract This paper presents studies on the subunit structure of Escherichia coli DNA-dependent RNA polymerase. Phosphocellulose column purified enzyme is denatured and its polypeptide chains separated by gel filtration Sephadex G-200 in presence 1% sodium dodecyl sulfate. The amino acid compositions, molecular weights, NH2 terminal acids, molar ratios these are presented. It concluded that phosphocellulose has α2ββ' where weights α, β, β' 39,000 ± 5%, 155,000 10%, 165,000 respectively. In...

10.1016/s0021-9258(18)63521-5 article EN cc-by Journal of Biological Chemistry 1969-11-01

We show, using dot matrix comparisons and statistical analysis of sequence alignments, that seven sequenced sigma factors, E.coli sigma-70 sigma-32, B.subtilis sigma-43 sigma-29, phage SP01 gene products 28 34i T4 product 55, comprise a homologous family proteins. Sigma-70, each have two copies similar to the helix-turn-helix DNA binding motif seen in CRP, lambda repressor cro gp28, gp34 at least one copy this sequence. propose second sequence, conserved all proteins i s core RNA polymerase...

10.1093/nar/14.16.6745 article EN Nucleic Acids Research 1986-01-01

Journal Article The codon preference plot: graphic analysis of protein coding sequences and prediction gene expression Get access Michael Gribskov, Gribskov McArdle Laboratory for Cancer Research, University Wisconsin-MadisonMadison, WI 53706, USA Search other works by this author on: Oxford Academic PubMed Google Scholar John Devereux, Devereux 1Laboratory Genetics, Wisconsin-Madison, MadisonWI Richard R. Burgess Nucleic Acids Volume 12, Issue 1Part2, 11 January 1984, Pages 539–549,...

10.1093/nar/12.1part2.539 article EN Nucleic Acids Research 1984-01-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPurification and properties of the .sigma. subunit Escherichia coli DNA-dependent RNA polymerasePeter A. Lowe, Dayle Hager, Richard R. BurgessCite this: Biochemistry 1979, 18, 7, 1344–1352Publication Date (Print):April 1, 1979Publication History Published online1 May 2002Published inissue 1 April 1979https://pubs.acs.org/doi/10.1021/bi00574a034https://doi.org/10.1021/bi00574a034research-articleACS PublicationsRequest reuse permissionsArticle...

10.1021/bi00574a034 article EN Biochemistry 1979-04-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTLarge-scale purification of wheat germ DNA-dependent RNA polymerase IIJerome J. Jendrisak and Richard R. BurgessCite this: Biochemistry 1975, 14, 21, 4639–4645Publication Date (Print):October 1, 1975Publication History Published online1 May 2002Published inissue 1 October 1975https://pubs.acs.org/doi/10.1021/bi00692a012https://doi.org/10.1021/bi00692a012research-articleACS PublicationsRequest reuse permissionsArticle...

10.1021/bi00692a012 article EN Biochemistry 1975-10-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTReplacement of potassium chloride by glutamate dramatically enhances protein-DNA interactions in vitroSigrid Leirmo, Catherine Harrison, D. Scott Cayley, Richard R. Burgess, and M. Thomas Record, Jr.Cite this: Biochemistry 1987, 26, 8, 2095–2101Publication Date (Print):April 1, 1987Publication History Published online1 May 2002Published inissue 1 April...

10.1021/bi00382a006 article EN Biochemistry 1987-04-01

We have determined the nudeotide sequence of rpoD gene which codes for sigma subunit RNA polymerase from E. coli K12. The gene, we formerly cloned as a Bindlll restriction fragment in transducing phage, Charon 25, was recloned into several plasmids. 2600 base pair DNA includes entire structural sigma. resulting amino acid agrees with previous information obtained about including theamino composition, partial data N-terminus, highly acidic nature polypeptide, and cleavage pattern at...

10.1093/nar/9.12.2889 article EN Nucleic Acids Research 1981-01-01

Wheat germ RNA polymerase II was used to raise monoclonal antibodies (mAbs) that cross-react with the largest subunit of calf thymus II. Most these mAbs were IgM isotype and shown react a synthetic peptide containing consensus sequence for C-terminal heptapeptide repeat has been found on from variety eukaryotic organisms. A representative mAb (3WG2) tested its effect transcription in both vitro vivo systems. Antibody 3WG2 did not affect (elongation) wheat denatured DNA. When HeLa cell...

10.1016/s0021-9258(18)60493-4 article EN cc-by Journal of Biological Chemistry 1989-07-01

Journal Article Nucleotide sequence preference at rat liver and wheat germ type 1 DNA topoisomerase breakage sites in duplex SV40 Get access Michael D. Been, Been 1Department of Microbiology Immunology. School Medicine. University WashingtonSeattle, WA 98195, USA Search for other works by this author on: Oxford Academic PubMed Google Scholar Richard R. Burgess, Burgess 2McArdle Laboratory Cancer Research, WisconsinMadison. WI 53709, James J. Champoux Nucleic Acids Volume 12, Issue 7, 11...

10.1093/nar/12.7.3097 article EN Nucleic Acids Research 1984-01-01

Active eukaryotic RNA polymerase II (RNAP II) was purified by immunoaffinity chromatography, using a monoclonal antibody (mAb) that reacts with the highly conserved heptapeptide repeat of largest subunit. This mAb (designated SWG16) conjugated to CNBr-activated Sepharose and used purify RNAP from wheat germ calf thymus. The subunit composition immunoaffinity-purified enzyme essentially same as conventional chromatography except it contained only form unproteolyzed could be eluted...

10.1016/s0021-9258(19)39260-9 article EN cc-by Journal of Biological Chemistry 1990-04-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTNonspecific interactions of Escherichia coli RNA polymerase with native and denatured DNA: differences in the binding behavior core holoenzymePieter L. DeHaseth, Timothy M. Lohman, Richard R. Burgess, Thomas Record, Jr.Cite this: Biochemistry 1978, 17, 9, 1612–1622Publication Date (Print):May 2, 1978Publication History Published online1 May 2002Published inissue 2...

10.1021/bi00602a006 article EN Biochemistry 1978-05-02
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