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Author

Jan Dijk

Bio: Jan Dijk is an academic researcher from Max Planck Society. The author has contributed to research in topics: Ribosomal protein & Ribosome. The author has an hindex of 16, co-authored 31 publications receiving 1077 citations.

Papers
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Journal ArticleDOI
02 Aug 1984-Nature
TL;DR: The 3-Å structure of DNA-binding protein II, which exhibits histone-like properties in bacteria, has been determined and a mechanism by which the protein induces DNA supercoiling is proposed.
Abstract: The 3-A structure of DNA-binding protein II, which exhibits histone-like properties in bacteria, has been determined. The molecule is dimeric and appears to bind to the phosphate backbone of DNA through two symmetry-related arms. A mechanism by which the protein induces DNA supercoiling is proposed.

308 citations

Book ChapterDOI
TL;DR: These methods are developed to isolate proteins from the Escherichia coli ribosome that are in a more native state than those that are previously isolated in the presence of acetic acid and urea.
Abstract: Publisher Summary The chapter discusses the purification of ribosomal proteins from Escherichia coli under nondenaturing conditions. These methods are developed to isolate proteins from the Escherichia coli ribosome that are in a more native state than those that are previously isolated in the presence of acetic acid and urea. The term “native” does not necessarily imply that the purified proteins are in the same conformational state as they are to be found in Situ on the ribosome because under these conditions protein-protein and protein-RNA interactions certainly play an important part. The conditions used for this purification procedure do not involve protein denaturants such as urea and extreme pH or lyophilization, but employ a high-salt extraction with LiCl followed by fractionation in the presence of salt. High salt concentrations especially of LiC1 are known to perturb the tertiary structure of proteins. The salt-extracted proteins are more soluble at high ionic strength and less soluble at low salt concentrations. This is the reverse of the solubility exhibited by previously prepared ribosomal protein.

92 citations

Journal ArticleDOI
Rudi Lurz1, Mathias Grote1, Jan Dijk1, Richard Reinhardt1, B. Dobrinski1 
TL;DR: DNA‐protein complexes formed in vitro with isolated DNA‐binding proteins from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius were analyzed by electron microscopy and two of the proteins formed specific structures after incubation with DNA.
Abstract: DNA-protein complexes formed in vitro with isolated DNA-binding proteins from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius were analyzed by electron microscopy. Two of the proteins (10a and 10b) formed specific structures after incubation with DNA. Protein 10a, at low protein concentrations, showed individual small spots on the DNA and at high concentrations evenly covered doublestranded DNA. Protein 10b showed three different types of regular structures: one with single-stranded and two with double-stranded DNA. Using double-stranded DNA, 10b first bound cooperatively to two strands forming long, plait-like structures only slightly shorter than respective free DNA. The complex consists of two right-handed, interwound fibers, with a helical pitch of 26 nm and a diameter of approximately 10-11 nm. At higher protein concentration than needed to package all DNA into the complex with two double-stranded DNAs, the two DNAs were separated again and a new structure was formed evenly covering only one DNA strand. Both structures showed no significant contraction of the length of the DNA covered in the complex. Nucleoprotein formed with single-stranded PhiX174 DNA had a diameter of approximately 11 nm and could form circles with a contour length of 0.5 mum.

88 citations

Journal ArticleDOI
TL;DR: Ribosomal and DNA binding proteins have been extracted from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius grown at 75–80°C and pH 4.8-4.5 and the DNA binding character of these proteins was verified using several binding assays.

82 citations

Journal ArticleDOI
Makoto Kimura1, Junko Kimura1, Philippa Davie1, Richard Reinhardt1, Jan Dijk1 
TL;DR: The thermoacidophilic archaebacterium Sulfolobus solfataricus possesses several DNA binding proteins which may have a histone‐like function, and one of the small proteins which occurs in a relatively large amount is purified and its amino acid sequence is determined.

54 citations


Cited by
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Journal ArticleDOI
TL;DR: Major advances in knowledge of transcriptional regulation involve the chromatin template, the large complexes recruited by transcriptional activators that regulate chromatin structure and the transcription apparatus, the holoenzyme forms of RNA polymerase II involved in initiation and elongation, and the mechanisms that link mRNA processing with its synthesis.
Abstract: ▪ Abstract The past decade has seen an explosive increase in information about regulation of eukaryotic gene transcription, especially for protein-coding genes. The most striking advances in our knowledge of transcriptional regulation involve the chromatin template, the large complexes recruited by transcriptional activators that regulate chromatin structure and the transcription apparatus, the holoenzyme forms of RNA polymerase II involved in initiation and elongation, and the mechanisms that link mRNA processing with its synthesis. We describe here the major advances in these areas, with particular emphasis on the modular complexes associated with RNA polymerase II that are targeted by activators and other regulators of mRNA biosynthesis.

934 citations

Journal ArticleDOI
06 Apr 1990-Cell
TL;DR: A cDNA clone that codes for a new tissue-specific DNA binding protein, PU.1, was isolated and was shown to be a transcriptional activator that is expressed in macrophages and B cells.

923 citations

Journal ArticleDOI
TL;DR: DNA bending induced by the H MG domain can facilitate the formation of higher-order nucleoprotein complexes, suggesting that HMG domain proteins may have an architectural role in assembling such complexes.

804 citations

Journal ArticleDOI
27 Dec 1996-Cell
TL;DR: The crystal structure of IHF complexed with 35 bp of DNA is reported, providing evidence for the importance of a narrow minor groove in IHF's binding sequence.

780 citations