A plant DNA-binding protein increases the number of active preinitiation complexes in a human in vitro transcription system.

We describe a partially fractionated in vitro transcription system from Xenopus laevis for the assay of transcription termination by RNA polymerase I. Termination in vitro was found to require a specific terminator sequence in the DNA and a DNA-binding protein fraction that produces a footprint over the terminator sequence.

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In vitro transcription directed from the somatostatin promoter is dependent upon a purified 43-kDa DNA-binding protein.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.86.7.2181 ◽

1989 ◽

Vol 86 (7) ◽

pp. 2181-2185 ◽

Cited By ~ 22

Author(s):

O. M. Andrisani ◽

Z. N. Zhu ◽

D. A. Pot ◽

J. E. Dixon

Keyword(s):

Dna Binding ◽

Binding Protein ◽

Dna Binding Protein ◽

In Vitro Transcription

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A DNA-binding protein is required for termination of transcription by RNA polymerase I in Xenopus laevis

Molecular and Cellular Biology ◽

10.1128/mcb.10.6.2793-2800.1990 ◽

1990 ◽

Vol 10 (6) ◽

pp. 2793-2800

Author(s):

B McStay ◽

R H Reeder

Keyword(s):

Dna Binding ◽

Xenopus Laevis ◽

Rna Polymerase ◽

Binding Protein ◽

Dna Binding Protein ◽

In Vitro Transcription ◽

Rna Polymerase I ◽

Polymerase I ◽

Terminator Sequence

We describe a partially fractionated in vitro transcription system from Xenopus laevis for the assay of transcription termination by RNA polymerase I. Termination in vitro was found to require a specific terminator sequence in the DNA and a DNA-binding protein fraction that produces a footprint over the terminator sequence.

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A plant DNA-binding protein that recognizes 5-methylcytosine residues.

Molecular and Cellular Biology ◽

10.1128/mcb.9.3.1351 ◽

1989 ◽

Vol 9 (3) ◽

pp. 1351-1356 ◽

Cited By ~ 20

Author(s):

D L Zhang ◽

K C Ehrlich ◽

P C Supakar ◽

M Ehrlich

Keyword(s):

Dna Binding ◽

Dna Sequence ◽

Base Pair ◽

Binding Protein ◽

Dna Binding Protein ◽

Sequence Specificity ◽

Dna Sequence Specificity ◽

Plant Dna ◽

Related Family ◽

Nuclear Extracts

A novel, 5-methylcytosine-specific, DNA-binding protein, DBP-m, has been identified in nuclear extracts of peas. DBP-m specifically recognizes 5-methylcytosine residues in DNA without appreciable DNA sequence specificity, unlike a mammalian DNA-binding protein (MDBP), which recognizes 5-methylcytosine residues but only in a related family of 14-base-pair sequences.

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The DNA-binding protein HTa from Thermoplasma acidophilum is an archaeal histone analog

eLife ◽

10.7554/elife.52542 ◽

2019 ◽

Vol 8 ◽

Cited By ~ 3

Author(s):

Antoine Hocher ◽

Maria Rojec ◽

Jacob B Swadling ◽

Alexander Esin ◽

Tobias Warnecke

Keyword(s):

Dna Binding ◽

Binding Protein ◽

Dna Binding Protein ◽

Coli Strain ◽

Micrococcal Nuclease ◽

Thermoplasma Acidophilum ◽

Chromatin Architecture ◽

Archaeal Histone

Histones are a principal constituent of chromatin in eukaryotes and fundamental to our understanding of eukaryotic gene regulation. In archaea, histones are widespread but not universal: several lineages have lost histone genes. What prompted or facilitated these losses and how archaea without histones organize their chromatin remains largely unknown. Here, we elucidate primary chromatin architecture in an archaeon without histones, Thermoplasma acidophilum, which harbors a HU family protein (HTa) that protects part of the genome from micrococcal nuclease digestion. Charting HTa-based chromatin architecture in vitro, in vivo and in an HTa-expressing E. coli strain, we present evidence that HTa is an archaeal histone analog. HTa preferentially binds to GC-rich sequences, exhibits invariant positioning throughout the growth cycle, and shows archaeal histone-like oligomerization behavior. Our results suggest that HTa, a DNA-binding protein of bacterial origin, has converged onto an architectural role filled by histones in other archaea.

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