Zolla Lello


Responsabile dell'U.O.

Cognome e Nome

Zolla Lello

Qualifica

PO

Dipartimento

Environmental Sciences (DISA)

Settore scientifico disciplinare

BIO/011

E-mail

zolla@unitus.it

Telefono

Personale strutturato

Cognome e Nome

Timperio Anna Maria

Qualifica

Ricercatore

Dipartimento

Environmental Sciences (DISA)

Ente di appartenenza

Tuscia University

Cognome e Nome

Vinciguerra Vittorio

Qualifica

Ricercatore

Dipartimento

Environmental Sciences (DISA)

Ente di appartenenza

Tuscia University

Cognome e Nome

Zolla Lello

Qualifica

PO

Dipartimento

Environmental Sciences (DISA)

Ente di appartenenza

Tuscia University

Personale non strutturato

Cognome e Nome

Ciambella Corrado

Qualifica

Post-doc

Dipartimento

Environmental Sciences (DISA)

Ente di appartenenza

Tuscia University

Cognome e Nome

D’Amici Giammaria

Qualifica

Ph.D student

Dipartimento

Environmental Sciences (DISA)

Ente di appartenenza

Tuscia University

Cognome e Nome

Faggioni Marco

Qualifica

Ph.D student

Dipartimento

Environmental Sciences (DISA)

Ente di appartenenza

Tuscia University

Cognome e Nome

Latini Arianna

Qualifica

Ph.D student

Dipartimento

Environmental Sciences (DISA)

Ente di appartenenza

Tuscia University

Cognome e Nome

Rinalducci Sara

Qualifica

Post-doc

Dipartimento

Environmental Sciences (DISA)

Ente di appartenenza

Tuscia University

Cognome e Nome

Rosetto Francesca

Qualifica

Borsista

Dipartimento

Environmental Sciences (DISA)

Ente di appartenenza

Tuscia University

Linee di ricerca

Nowadays mass spectrometry is a powerful tool used to study, by a proteomic approach, the protein content and its function in different biological systems. Our investigations concern the study of cell proteins, in both animal and plant kingdom, that could be over- or under-expressed upon stress conditions or after chemical and therapeutic treatments 1. Plant systems 1.1 Proteomic of plants, algae and cyanobacteria under environmental stress conditions Proteomic mapping of the photosynthetic apparatus from plants, algae and cyanobacteria allows us to check if any change in the environmental conditions can result as a consequence of the adaptation. Thus, comparing untreated organism with one grown in stress conditions (water stress, light stress, heavy metals stress, temperature stress) it is possible to identify which are the main proteins involved and how the organism could be genetically modified; this gives the opportunity to obtain resistant organisms, hence to improve the productivity of determined crops. 1.2 Proteomic of genetically modified organisms (GMO): Three Zea mays lines (MON-810, Bt11, Bt176) have been developed by specific genetic modifications to become resistant to European corn borer (ECB): Ostrinia nubilalis. In this case the main aim of the research is to identify which are the changes of protein expression due to new gene insertion. 2 Animal systems 2.1 Proteomic of different pancreatic tumoral cell strains after drug treatment Pancreatic tumoral cell strains have been treated (separately or in combination) with drugs acting on the tumor epigenetic events (e.g. histone deacetylation, DNA hypermethylation). The proteomic analysis is focused on the identification of differential expressed proteins after drugs treatment. The study of activation/repression levels of the involved proteins results in an increased knowledge of growth processes and cell apoptotic response. 2.2 Proteomic of erythrocytes membranes and cell aging These studies are focused on the characterization of proteic pattern changes following the oxidative events due to cell aging during the common blood storage. 2.3 Proteomic of mammary glands of different cows The aim of this differential proteomic is the identification of specific proteins that could be potentially responsible of the biodiversity of cow races used for milk production.

Tecnologie in uso dall'UO

  1. 1.
    Protein separation by 2-D electrophoresis and by high performance liquid chromatography.
  2. 2.
    Protein identification by PMF (Peptide Mass Fingerprinting), Sequence-Tag and IMM (Intact Molecular Mass).
  3. 3.
    DNA fragment separation and SNPs identification by mass-spectrometry.
  4. 4.
    Oxigen Singlet determination by EPR.
  5. 5.
    Membrane Proteins separation and identification.
  6. 6.
    Monolith capillary column for nano-HPLC separation.

Strumentazione

Denominazione

Mass Spectrometer micro-TOF-Q Bruker
Mass Spectrometer HCT plus Bruker
Mass Spectrometer Esquire 3000 plus Bruker
Mass spectrometer MALDI-TOF Biflex III Bruker
ESP 300 spectrometer Bruker
Two Ultracentrifuges (Beckman and Kontron)
Two HPLC (Beckman Gold System and Pelkin Elmer)
Two nano-HPLC Dionex
Spectrophotometer UV-Vis Cary 4 Varian
Etan Dalt Six 2D-gel system Amersham Biosciences

Struttura ove la strumentazione è allocata

Proteomic and Genomic Lab. (DISA)
Proteomic and Genomic Lab. (DISA)
Proteomic and Genomic Lab. (DISA)
Proteomic and Genomic Lab. (DISA)
Proteomic and Genomic Lab. (DISA)
Proteomic and Genomic Lab. (DISA)
Proteomic and Genomic Lab. (DISA)
Proteomic and Genomic Lab. (DISA)
Proteomic and Genomic Lab. (DISA)
Proteomic and Genomic Lab. (DISA)

Responsabile

Prof. Zolla
Prof. Zolla
Prof. Zolla
Prof. Zolla
Prof. Zolla
Prof. Zolla
Prof. Zolla
Prof. Zolla
Prof. Zolla
Prof. Zolla

Pubblicazioni

  1. 1.
    Rinalducci S., Campostrini N., Antonioli P., Righetti P. G., Roepstorff P., Zolla L. Formation of truncated proteins and high-molecular-mass aggregates upon soft illumination of photosynthetic proteins. J Proteome Res. 2005; 4:2327-37
  2. 2.
    Timperio A. M., Zolla L. Investigation of the lateral light-induced migration of photosystem II light-harvesting proteins by nano-high performance liquid chromatography electrospray ionization mass spectrometry. J Biol Chem. 2005; 280: 28858-66.
  3. 3.
    Gil-Augusti M.T., Campostrini N., Zolla L., Ciambella C., Invernizzi C., Righetti P.G. Two-dimensional mapping as a tool for classification of green coffee bean species. Proteomics. 2005; 5: 710-8.
  4. 4.
    Monacelli B., Pasqua G., Botta B., Vinciguerra V., Gacs-Baitz E., Delle Monache G. "Abietane Diterpenoids from callus cultures of taxus bacata". Planta Med. 2002; 68: 764-766.
  5. 5.
    Zolla L., Rinalducci S. Involvement of active oxygen species in degradation of light-harvesting proteins under light stresses. Biochemistry. 2002; 48: 14391-402
  6. 6.
    Huber C.G., Timperio A. M., Zolla L. Isoforms of photosystem II antenna proteins in different plant species revealed by liquid chromatography-electrospray ionization mass spectrometry. J Biol Chem. 2001; 276: 45755-61.
  7. 7.
    Zolla L., Rinalducci S., Timperio A. M., Huber C.G., Righetti P.G. Intact mass measurements for unequivocal identification of hydrophobic photosynthetic photosystems I and II antenna proteins. Electrophoresis. 2004; 25:1353-66.
  8. 8.
    Huber C.G., Walker W., Timperio A. M., Troiani S., Porceddu A, Zolla L. Multidimensional proteomic analysis of photosynthetic membrane proteins by liquid extraction-ultracentrifugation-liquid chromatography-mass spectrometry. Proteomics. 2004; 4:3909-20.
  9. 9.
    Walker W., Timperio A. M., Zolla L., Huber C. G. Characterization of a variant of the spinach PSII type I light-harvesting protein using kinetically controlled digestion and RP-HPLC-ESI-MS. Anal Chem. 2003; 75:6775-80.
  10. 10.
    Zolla L., Rinalducci S., Timperio A. M., Huber C. G. Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry. Photosystem I. Plant Physiol. 2002;130:1938-50.

Dottorandi di ricerca

Componente UO

Zolla Lello
Timperio Anna Maria

Dottorato di ricerca

Genetics and Molecular Biology
Genetics and Molecular Biology

Coordinatore

Prof. Prantera Giorgio Dept. Environ. Sciences
Prof. Prantera Giorgio Dept. Environ. Sciences

Sede

University
University