Influence of HgCl2 on the expression of fibrillarin (Fb) in germination of Phaseolus vulgaris LFibrilarina
Keywords:
Fibrilarin, Mercuric chloride, Western blot, proteins, germinationAbstract
Mercury (Hg) is now considered an environmental contaminant of high risk to human health and the environment. The toxicity of mercury and its compounds has been extensively documented, but the molecular mechanisms of tox- icity have not been fully clarified. The aim of this study was to analyze the effect of mercuric chloride (HgCl2) in the expression of Fb, as a biomarker of early effect of mercury contamination, using as a model of Phaseolus vulgaris L. seeds, black variety Jamapa . Fibrillarin (Fb) one of the main components of the nucleolus, is an essential ribonucleo- protein phylogenetically conserved in ribosomal RNA processing (rRNA) in partnership with small nucleolar RNAs (snoRNAs), along with other basic functions in biological systems. The expression of Fb was monitored by protein electrophoresis (SDS-PAGE) and Western blot of embryos beans during early stages of germination with different times 0, 6, 12, 18, 24 and 30 hrs and exposure 10 , 20 and 30 µM HgCl2. The results obtained by Western blot re- vealed that inhibits mercury nucleolar protein expression Fb from a minimum concentration of 10 µM HgCl2 after 18 hours after the start of germination. These observations demonstrate that the protein is usually a mercury target mole- cule capable of inhibiting its expression. This particular selectivity of HgCl2 by protein may constitute the biochemi- cal basis for considering Fb as early biomarker of contamination by HgCl2 Additionally the results show that the inhi- bition HgCl2 and caused marked delay seed germination gradually, as the dose of mercury is increased to 30 µM HgCl2.
References
Barceló, J. y Poschenrieder, C. (2003). Phytoremediation: principles and perspectivas. Contributions to Science, 2 (3), 333-344.
Baserga, S.J., Yang X.D. y Steitz J.A. (1991). An intact box C sequence in the U3 snRNA is required for binding of fibrillarin, the protein common to the major family ofnucleolar snRNPs. EMB0, (10), 2645–2651.
Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein. Ana- lytical Biochemistry, 72, 248-255.
Cerdido, A. y Medina F.J. (1995). Subnucleolar location of fibrillarin and variation in its levels during the cell cycle and during differentiation of plant cells. Chromosoma, 103, 625-634.
Costa, G. y Spitz E. (1997). Influence of cadmium on solu- ble carbohydrates, free amino acids, proteins content of in vitro cultured Lupinus albus. Plant Science, 128, 131-140. Chen, M., Rockel, T., Steinweger, G., Hemmerich, P., Risch
J. y von Mikecz, A. (2002) Subcellular Recruitment of Fibrillarin to Nucleoplasmic Proteasomes: Implications for Processing of a Nucleolar Autoantigen. Molecular Biology of the Cell. 13(10), 3576-87.
Chen, M. y von Mikecz, A. (2005). Xenobiotic-induced recruitment of atuantigens to nuclear proteasomes sug- gests a role for altered antigen in Scleroderma. Annals of the New York Academy of Sciences, 1051, 382-389
Ericson, M.C. y Alfinito, A.E. (1984). Proteins produced during salt stress in tobacco cell cultures. Plant Physiology, 74, 506-509.
Garcia, E.M. y Reyes, R.E. (2001). Synthesis pattern of an Hg-binding protein in Acetabularia calyculus during short-term exposure to mercury. Bulletin of Environmen- tal Contamination and Toxicology, 66, 357-364.
Guiltinan, M.J., Schelling, M.E., Ehtesham, N.Z., Thomas,
J.C. y Christensen, M.E. (1988). The nucleolar RNA- binding protein B-36 is highly conserved among plants. European Journal of Cell Biology, 46, 547-553.
Laemmli, U. K. (1970). Cleavaje of Structural Proteins during the Assembly of the Head Bacteriophage T4. Na- ture, 227, 680-685.
Nambara E, Naito S. y McCoort P. (1992). A Mutant of Arabidopsis wich is Defective in Seed Development Stor- age Protein Accumulation is a New abi3 Allele. The Plant Journal, 2(4), 435-441.
Navarro, A.R., Arrieta R.G., y Maldonado M.C. (2006). Determinación del efecto de diferentes compuestos a través de ensayos de fitotoxicidad usando semillas de lechuga, escarola y achicoria. Critical Reviews in Toxi- cology, 23, 125-129.
Palma, J.M., Sandalio, C.F., Romero-Puertas M.C. (2002). Plant Proteases protein degradation and oxidative stress: role of peroxisomes. Plant Physiology and Biochemistry, 40, 521-530.
Patra, M., Bhowmik N., Bandopadhyay, B. y Sharma, A. (2004) Comparison of mercury, lead and arsenic with respect to genotoxic effects on plant systems and the development of genetic tolerante. Environmental and Experimental Botany, 52, 199-223.
Pih, K. T., Yi, M. J., Liang, Y. S., Shin, B. J., Cho. M. J.,
Hwang, I. y Son D. (2000). Molecular Cloning and Tar- geting of a Fibrillarin Homolog from Arabidopsis. Plant Physiology, 123, 51-58
Pirrone, N., Costa P., Pacyna, J. M. y Ferrara, R. (2001). Atmospheric mercury emissions from anthropogenic sources in the Mediterranean Región. Atmospheric Envi- ronment, 35, 2997-3006.
Pollard, K. M., Lee, D. K. Casiano, C. A., Bluthner, M., Johnston, M. M. y Tan E. M. (1997). The Autoimmunity Inducing Xenobiotic Mercury Interacts with the Autoan- tigen Fibrillarin and Modifies Its Molecular and Anti- genic Properties. The Journal of Immunology, 158, 3521- 3528.
Pollard, K. M., Pearson, D. L. y Tan, E. M. (2000). Prote- olytic Cleavage of a Self-Antigen Following Xenobiotic- Induced Cell Death Produces a Fragment with Novel Immunogenic Properties. The Journal of Immunology, 165, 2263–2270.
Programa de las Naciones Unidas para el Medio Ambiente. (2002). Evaluación Mundial sobre el Mercurio (Hg). Ginebra Suiza. (Versión español publicada Junio 2005), 2:32-53; 3:70-92; 4: 113-137.
Schurz F., Vilar M. S. y Gremmels J.F. (2000). Mutagenic- ity of mercury chloride and mechanisms of cellular de- fence: the role of metal-binding proteins. Mutagenesis, 15(6), 525-530.
Sipter E., Auerbach R., Katalin G. y Mathe-Gaspar G. (2009). Change of bioacumulation of toxic metals in vegetables. Communications in Soil Science and Plant Analysis, 40, 285-293.
Stepinski D. (2009) Immunodetection of nucleolar proteins and ultrastructure of nucleoli of soybean root meriste- matic cells treated with chilling stress and after recovery. Protoplasma, 235, 77-89.
Takeuchi, M., Rothe, M. y Goeddel, D. V. (1996). Anato- my of TRAF2. Distinct domains for nuclear factor- kappaB activation and association with tumor necrosis factor signaling proteins. The Journal of Biological Chemistry, 271, 19935-19942.
Towbin, H., Staehelin, T. y Gordon, J. (1979). La transfer- encia electroforética de las proteínas desde geles de poli- acrilamida a láminas de nitrocelulosa: procedimiento y algunas aplicaciones. Proceedings of the National Acade- my of Sciences EE.UU, 76, 4350-4354
Towbin, H. y Gordon, J. (1984). Immunoblotting and dot immunobinding. Curret status and outlook. Journal of Immunological Methods, 72, 312.
Wilson, J.K. (1915). Calcium hypochlorite as a seed steri- lizer. American Journal of Botany, 2, 420-427
Downloads
Published
Data Availability Statement
No
Issue
Section
Categories
License
Copyright (c) 2026 Josefina Huerta , Edgar León Esparza , Francisco Javier Cabral , Lucía Delgadillo (Autor/a)

This work is licensed under a Creative Commons Attribution 4.0 International License.
This work is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License.
Open Access Statement as defined by DOAJ
“Open Access” is a general term encompassing both Free and Open Access. For DOAJ, open access is only when digital content is freely available online and user rights and copyright terms are clearly defined.
All texts published by Tlamati—without exception—are distributed under the Creative Commons Attribution-ShareAlike 4.0 International License.
Authors may enter into separate, additional contractual agreements for the non-exclusive distribution of the version of the article published in Science and Philosophy ISSN: 2594-2204 (for example, including it in an institutional repository or publishing it in a book), provided they clearly indicate that the work was first published in Tlamati.
This is a human-readable summary of (and not a substitute for) the license.
You are free to:
Share
Read
Download
Translate
Copy
Distribute
Print
Search or link to the full text of the articles
Crawl them for indexing
Pass them as data into software or
Use them for any other lawful purpose, in any medium or format
License terms: https://creativecommons.org/licenses/by-sa/4.0/deed.es
You are free to:
Share — copy and redistribute the material in any medium or format for any purpose, even commercially.
Adapt — remix, transform, and build upon the material for any purpose, even commercially. The licensor cannot revoke these freedoms as long as you follow the license terms.
Under the following terms:
Attribution — You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.
ShareAlike — If you remix, transform, or build upon the material, you must distribute your contributions under the same license as the original.
No additional restrictions — You may not apply legal terms or technological measures that legally restrict others from doing anything the license permits.
