Interaction of a low mobility group protein, LMG160, with deoxyribonucleic acid

Low mobility group nonhistone protein, LMG(160), is a ribonucleoprotein particle of the nuclear matrix with an inhibitory effect on transcription. Through the current study, we have investigated comparatively the effect and behavior of the protein in the absence and presence of its RNA moiety. Analysis was performed with the intact LMG(160) and its RNase-treated form using native and denatured gel electrophoresis as well as fluorescence spectroscopy and trypsin digestion techniques. The results show that the RNA moiety of LMG(160) plays a key role in maintaining the overall structure and conformation of this RNP particle, in the way that RNA removal causes some alterations in the structural stability of the protein, leading it to become self-associated. This finding can easily explain the loss of function of LMG(160) after RNase-treatment, the effect that may influence the biological activity of the molecule in the nuclear matrix structure.

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Evidence for the structural stability of ribonucleoprotein LMG160 under ribonuclease-A treatment

Shahhoseini

Chadegani

Abdosamadi

2008

Mol Cell Biochem

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Transcriptional inhibition by a non-histone protein from low mobility group in homologous and heterologous in vitro systems

Shahhoseini

Rabbani-Chadegani

2007

Mol Biol Rep

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An acidic non-histone chromosomal protein of low mobility group (LMG) with pI of 5-5.5 and molecular weight of 160 kDa (named LMG160), has been isolated from rat liver nuclei and its inhibitory effect on transcription of DNA in vitro has been detected in a heterologous prokaryotic in vitro transcription system (T7 RNA polymerase) and also confirmed in the homologous cell-free system of rat liver nuclear extract. The results indicate that in the presence of non-histone protein LMG160, in vitro RNA synthesis represses in the both systems, which can suggest a functional role for this non-histone chromosomal protein.

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Identification of nonhistone protein LMG160 as a ribonucleoprotein of the nuclear matrix with a role in transcription in vitro

2007

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Interaction of a low mobility group protein, LMG160, with deoxyribonucleic acid

Cited by 3 publications

References 10 publications

Evidence for the structural stability of ribonucleoprotein LMG160 under ribonuclease-A treatment

Evidence for the structural stability of ribonucleoprotein LMG160 under ribonuclease-A treatment

Transcriptional inhibition by a non-histone protein from low mobility group in homologous and heterologous in vitro systems

Identification of nonhistone protein LMG160 as a ribonucleoprotein of the nuclear matrix with a role in transcription in vitro

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