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

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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Insights into the structural stability of nuclear matrix ribonucleoprotein, LMG₁₆₀: thermodynamic and spectroscopic analysis

Abdossamadi

Rabbani-Chadegani

Shahhoseini

2013

Journal of Biomolecular Structure and Dynamics

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Low-mobility group nonhistone chromatin protein, LMG160, is a nuclear matrix ribonucleoprotein particle (RNP) which has a RNA molecule with approximately 300 bases. In this study, structural stability of the intact LMG160 (I-LMG160) was investigated at different ionic strength and in the absence of its RNA moiety (T-LMG160) employing spectroscopic and thermodynamic techniques. The UV absorption spectra showed hypochromicity and red shift under increasing ionic strength for both forms of LMG160 but in different extents. The fluorescence emission intensity was decreased as ionic strength was increased and the Stern-Volmer quenching constant (Ksv) for T-LMG160 was 3.7 times less than for I-LMG160. In the absence of sodium chloride, I-LMG160 exhibited a very stable structure against the temperature change compared to T-LMG160. The thermodynamic parameters showed that the positive values of ΔHm and ΔSm increased by increasing ionic strength in both forms of LMG160. Removal of the RNA moiety altered secondary structure: as T-LMG160 showed more helical content than I-LMG160. From the results, it is concluded that I-LMG160 is more sensitive to alteration of environment and the RNA has an important role in this RNP conformation. Also, interaction of both I- and T-LMG160 with sodium chloride is entropy driven and is usually accompanied by surface hydrophobicity.

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

Cited by 2 publications

References 22 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

Insights into the structural stability of nuclear matrix ribonucleoprotein, LMG₁₆₀: thermodynamic and spectroscopic analysis

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

Cited by 2 publications

References 22 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

Insights into the structural stability of nuclear matrix ribonucleoprotein, LMG160: thermodynamic and spectroscopic analysis

Contact Info

Product

Resources

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Insights into the structural stability of nuclear matrix ribonucleoprotein, LMG₁₆₀: thermodynamic and spectroscopic analysis