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Institute of Biosciences and Bioresources

National Research Council of Italy

Beatrice Cobucci-Ponzano

Role: Researcher
Section: Researchers and Technologists
Division: Naples
Tel: (39) 081-6132564
E-mail: beatrice.cobucciponzano@ibbr.cnr.it


Address

Dr. Beatrice Cobucci-Ponzano

Researcher

Via P. Castellino 111, 80131 Naples ITALY

tel. +39 081 6132564 (direct); +39 081 6132563 (lab)

e-mail: beatrice.cobucciponzano@ibbr.cnr.it

Research Interests

We are interested since long time in the study of enzymes involved in the hydrolysis and synthesis of glycosides. Our model systems are the enzymes from (hyper)thermophilic microorganisms, mainly Archaea, which are considered the extant organisms closest to the early forms of life on Earth. In particular, our studies are focused on the understanding of the structure/function relationship of these hyperthermophilic proteins and enzymes and on the mechanicistic aspects of the enzymatic hydrolysis of glycosides. More recently, we started a new research’s line on the mechanism of expression and the role of some of these genes in vivo.

Current Projects

The group’s major projects are:

  • Cloning and expression of genes encoding carbohydrate active enzymes (da collegare al link http://www.cazy.org/) for their detailed biochemical characterization and for their exploitation in biotechnological applications (agro-food, biofuels, pharmaceutical industry).
  • Modification and detailed kinetic characterization of hyperthermophilic glycoside hydrolases to understand their reaction mechanism, the catalytic machinery, the substrate specificity and to identify the molecular determinants responsible of thermal activity and thermostability.
  • Production of engineered glycosidases, which synthesise, but do not degrade oligosaccharides (glycosynthases). These mutant enzymes have interesting potential applications in pharmaceutical industry and in bio-medicine.
  • Study of possible functional interactions among different carbohydrate active enzymes to clarify their role in vivo
  • Cultivation of hyperthermophiles to study the mechanisms of gene expression in Archaea (da collegare al link http://www-archbac.u-psud.fr/projects/sulfolobus/) at transcriptional and translational level to understand the basic mechanisms of the transfer of genetic information and to trace the origin and evolution of life on Earth. These studies recently led to the identification, for the first time in Archaea, of the translational recoding event (da collegare al link http://recode.genetics.utah.edu/) named programmed -1 frameshifting.

Studied enzymes include b-glucosidases, b-galactosidases, a-L-fucosidases, a-mannosidases, a-xylosidases, b-glucanases and others. We use a variety of techniques, including microbiology, molecular biology, protein chemistry, site-directed mutagenesis, enzyme kinetics and inhibition. These approaches are coupled with organic chemistry in collaboration with collegues at the University of Naples “Federico II” (da collegare al link http://www.unina.it/). In addition, we are now approaching glycobiology and glycomic of the hyperthermophilic Archaea.

Key publications

Cobucci-Ponzano B, Moracci M. (2012) Glycosynthases as tools for the production of glycan analogs of natural produc... Nat Prod Rep. 29:697-709

Cobucci-Ponzano B, Aurilia V, Riccio G, Henrissat B, Coutinho PM, Strazzulli A, Padula A, Corsaro MM, Pieretti G, Pocsfalvi G, Fiume I, Cannio R, Rossi M, Moracci M. (2010) A new archaeal beta-glycosidase from Sulfolobus solfataricus: seeding a novel ... J Biol Chem. 285:20691-703

Cobucci-Ponzano B, Guzzini L, Benelli D, Londei P, Perrodou E, Lecompte O, Tran D, Sun J, Wei J, Mathur EJ, Rossi M, Moracci M. (2010) Functional characterization and high-throughput proteomic analysis of interrup... J Proteome Res. 9:2496-507.

Cobucci-Ponzano B, Conte F, Bedini E, Corsaro MM, Parrilli M, Sulzenbacher G, Lipski A, Dal Piaz F, Lepore L, Rossi M, Moracci M. (2009) beta-Glycosyl azides as substrates for alpha-glycosynthases: preparation of ef...

Chem Biol. 16:1097-108.

Cobucci-Ponzano B, Conte F, Benelli D, Londei P, Flagiello A, Monti M, Pucci P, Rossi M, Moracci M. (2006) The gene of an archaeal alpha-L-fucosidase is expressed by translational frame... Nucleic Acids Res. 34:4258-68.

Links

Carbohydrate Active EnZYmes (http://www.cazy.org/)

Sulfolobus solfataricus P2 genome (http://www-archbac.u-psud.fr/projects/sulfolobus/)

Translational Recoding (http://recode.genetics.utah.edu/)

Work experiences

2014. Researcher

CNR - Institute of Biosciences and BioResources, UOS Naples, Italy

2001. Researcher

CNR - Institute of Protein Biochemistry, Naples, Italy

2001. Ph.D. in Biochemistry and Biophysic

University of Padua, Padua, Italy.

1998. Fellow of the University of Naples “Federico II”

CNR - Institute of Protein Biochemistry, Naples, Italy

1997. Degree in Biological Sciences cum laude. Dissertation in Enzymology

University of Naples “Federico II” , Naples, Italy

Other professional experiences

2014 Member of the Local Organizing Commette of the First Workshop IBBR, Naples (Italy) 6-7 October 2014

2009. Member of the Local Organizing Commette of the 8th Carbohydrate Bioengineering Meeting (CBM8), Ischia, Naples (Italy) 10-13

May 2009

2005: Lecturer “Extremophilc organisms as alternative source of biomolecules” in Principles of genetic and metabolic engineering for the course of Regione Campania - POR 2000/2006 Experts in biotechnological industrial applications.

2003: Lecturer “Enzymes of industrial application: thermophilic enzymes” for the course of “Applicative Enzymology” Faculty of Biotechnology - University of Naples “Federico II”.

2002: lecturer “Molecular mechanisms of stabilization of proteins” for the course of “Applicative Enzymology” Faculty of Biotechnology - University of Naples "Federico II".

2001: Lecturer "Enzymes from thermophilic archaeon: molecular basis of thermostability" for the course "Industrial Microbiology" for the School of Specialization in Biotechnological Applications of University of Naples "Federico II".

 

Selected Publications
(full list available at CNR People)

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