TnpA product encoded by the transposable element En-1 of Zea mays is a DNA binding protein.

A. Gierl; S. Lütticke; H. Saedler

doi:10.1002/j.1460-2075.1988.tb03298.x

TnpA product encoded by the transposable element En-1 of Zea mays is a DNA binding protein.

A. Gierl, S. Lütticke, H. Saedler

Max-Planck-Institute for Plant Breeding Research

Research output: Contribution to journal › Article › peer-review

113 Scopus citations

Abstract

TnpA protein, the function encoded by the most abundant transcript of En-1 was expressed in Escherichia coli. DNA binding experiments with partially purified tnpA protein revealed that it binds to the subterminal repetitive region of En-1. TnpA protein recognizes a 12-bp-long sequence motif which is reiterated several times at the termini of En-1. Binding is reduced if the cytosine residues of CG dinucleotides and CNG trinucleotides within the motif are methylated. These data suggest a model in which the product of tnpA serves as a regulator of element activity.

Original language	English
Pages (from-to)	4045-4053
Number of pages	9
Journal	EMBO Journal
Volume	7
Issue number	13
DOIs	https://doi.org/10.1002/j.1460-2075.1988.tb03298.x
State	Published - 20 Dec 1988
Externally published	Yes

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10.1002/j.1460-2075.1988.tb03298.x

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title = "TnpA product encoded by the transposable element En-1 of Zea mays is a DNA binding protein.",

abstract = "TnpA protein, the function encoded by the most abundant transcript of En-1 was expressed in Escherichia coli. DNA binding experiments with partially purified tnpA protein revealed that it binds to the subterminal repetitive region of En-1. TnpA protein recognizes a 12-bp-long sequence motif which is reiterated several times at the termini of En-1. Binding is reduced if the cytosine residues of CG dinucleotides and CNG trinucleotides within the motif are methylated. These data suggest a model in which the product of tnpA serves as a regulator of element activity.",

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AU - Gierl, A.

AU - Lütticke, S.

AU - Saedler, H.

PY - 1988/12/20

Y1 - 1988/12/20

N2 - TnpA protein, the function encoded by the most abundant transcript of En-1 was expressed in Escherichia coli. DNA binding experiments with partially purified tnpA protein revealed that it binds to the subterminal repetitive region of En-1. TnpA protein recognizes a 12-bp-long sequence motif which is reiterated several times at the termini of En-1. Binding is reduced if the cytosine residues of CG dinucleotides and CNG trinucleotides within the motif are methylated. These data suggest a model in which the product of tnpA serves as a regulator of element activity.

AB - TnpA protein, the function encoded by the most abundant transcript of En-1 was expressed in Escherichia coli. DNA binding experiments with partially purified tnpA protein revealed that it binds to the subterminal repetitive region of En-1. TnpA protein recognizes a 12-bp-long sequence motif which is reiterated several times at the termini of En-1. Binding is reduced if the cytosine residues of CG dinucleotides and CNG trinucleotides within the motif are methylated. These data suggest a model in which the product of tnpA serves as a regulator of element activity.

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TnpA product encoded by the transposable element En-1 of Zea mays is a DNA binding protein.

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