Alessandra Albertini
Alessandra Albertini
affiliation: Università di Pavia
research area(s): Genetics And Genomics, Molecular Biology
Course: Genetics, Molecular and Cellular Biology
University/Istitution: Università di Pavia
ALESSANDRA ALBERTINI is full Professor of Genetics at the Faculty of Sciences of the University of Pavia since 2005.
Graduated in Biology in 1974 at the University of Pavia, in 1977 she obtained her Degree in Biophysics, Physics Specialization School, of the same University.
From 1975 to 1980 she was granted a Post-doctoral fellowship from the Italian Education Ministry (MPI) to work at Institute of Genetics of the University of Pavia.
From 1980 to 1982 she was granted of an EMBO Post-doctoral fellow at the Dep. of Molecular Biology at the University of Geneva, CH.
From 1983 to 1987 was Researcher at the Department of Genetics and Microbiology, University of Pavia.
In 1987-91 she was Associate Professor of Genetics, Faculty of Agricultural Sciences at the University of Udine.
From 1991 to 2005 she was Associate Professor of Molecular Genetics and Genetics for the Biological Sciences and Biotechnology Degrees, University of Pavia, Faculty of Sciences.
Her research interests concern the regulation of NAD synthesis in B. subtilis; expression and mutagenesis of heterologous proteins in bacteria (MUTYH, hMutY); expression, mutagenesis and immobilization of enzymes for biocatalysis (phosphorylases, acylases, ribonucleotide reductases); chromosomal technologies for Gram+; B. subtilis genome sequencing and systematic functional analysis; molecular genetics of Bacillus thuringiensis entomopathogenic toxin; expression and in vivo recombination of heterologous genes in Bacillus subtilis; regulation of the expression of genes involved in Bacillus subtilis spore germination and outgrowth; molecular origin of chromosomal amplification and deletion mutations in prokaryotes; informational extragenic suppression of non sense mutations in E. coli.
Together with A. Galizzi, she took part in two EU research projects, SCIENCE and BIOTECH, on Bacillus subtilis. She coordinated a MIUR PRIN project in 2000 and she participated to other two (PRIN 2002 and 2004).
She is Member of the American Society of Microbiology, the Italian Genetics Association, the Italian Microbiology and Microbial Biotechnology Association, referee for several international scientific journals (BMC Microbiology, Journal of Bacteriology, Applied and Environmental Microbiology, FEMS Microbiology Letters, Annals of Microbiology, Industrial biotechnology) and granting agencies (National Science Foundation, USA; Ministero Italiano dell’Università e Ricerca, University of Padua, Italy ).
The research unit is active in Microbial Genetics and Biotechnology following two main lines of research; one regarding the use of bacteria (Escherichia coli) has factories for the production of proteins from other sources, the second focused on mechanisms of gene expression regulation in Bacillus subtilis.

Bacterial cell factories for catalysts production and mutagenesis.

E. coli is well suited for the expression of foreign genes, due to the vast knowledge of its metabolism and the availability of a large collection of different vectors and strains. In the last years the group of Microbial Genetics and Biotechnology collaborated with the Biocatalysis Laboratory of the Departement of Pharmaceutical Chemistry of the University of Pavia for the production of new biocatalysts, such as PGA (Penicillin G acylase, catalyst for the production of β lactam nuclei), to be used for the synthesis of semi-synthetic antibiotics, or purine and pyrimidine phosphorylases, catalysts for the transglycosilation reactions between a nucleoside (natural or modified in the sugar moiety) and a natural or modified purine or pyrimidine base.
Aims of these projects are the production of new immobilized catalysts trough the search of new genes for purine and pyrimidine phosphorylases from different bacterial sources, and new strategies coupling in vitro site directed mutagenesis and immobilization for the rational design of more efficient acylase based biocatalysts.
Gene expression regulation in the model organism Bacillus subtilis.
The regulation of gene expression in B. subtilis has mainly been directed to the study of the early stationary phase behaviours and to the regulation of the genes involved in the NAD(H) de novo synthesis. Motility and γ-PGA production: the research group is interested in the production of the polymer poly-gamma-glutamate (γ-PGA) and the activation of a coordinated form of motility on semi-solid surfaces, known as swarming. The free γ-PGA polymer, or hydrogels and nanoparticles composed of it, are drawing together an increasing industrial interests. Their applications are ranging from waste water treatment, food preservation, up to drug delivery. γ-PGA synthesis has traditionally been associated with wild strains of Bacillus sp. In the last years few research groups in the world, including the DGM Microbial Genetics group, have identified the genetic determinants that allow a B. subtilis laboratory strain to display such “wild” behaviours.
The de novo synthesis of NAD, an important cofactor, essential in many organism, has been analyzed in Bacillus subtilis. In many eubacteria, including pathogens, the first steps of the de novo synthesis are catalyzed by L-aspartate oxidase (NadB), quinolinate synthase (NadA) and quinolinate phosphoribosyltransferase (NadC). In B. subtilis the synthesis of these enzymes is coregulated with that of a cysteine desulfurase (IscS), for the [Fe-S] cluster assembly. The transcription regulation of these pathways is studied by cloning and site directed mutagenesis of the promoter(s)-operator and of the YrxA/NiaR regulator, and by in vivo transcription analysis with gene-reporter fusions with different mutations in the regulator or in the operator. NadA and NadB have been over-expressed and characterized, obtaining informations on the NadA cofactor and its interaction with NadB. The NadA cofactor is a [4Fe-4S] cluster and for the first time the cysteines involved in the cluster binding have been identified. The results obtained show for the first time that the interaction between NadA and NadB is not species-specific and that the integrity of the Fe-S cluster may be important for the binding of iminoaspartate to NadA.
Serra I., Ubiali D., Cecchini D.A., Calleri E., Albertini A.M., Terreni M., Temporini C.
Assessment of immobilized PGA orientation via the LC-MS analysis of tryptic digests of the wild type and its 3K-PGA mutant assists in the rational design of a high-performance biocatalyst. Anal Bioanal Chem.DOI: 10.1007/s00216-012-6143-z, Jun 19, 2012

Ubiali D., Serra C.D., Serra I., Morelli C.F., Terreni M., Albertini A.M., Manitto P. and Speranza G. Production, characterization and synthetic applicatio of a purine nucleoside phosphorylase from Aereomonas hydrophyla. Adv Synth. Catal. 354, 96-1041, 2012.

D'Agostino V., Minoprio A., Torreri P., Marinoni I., Bossa C., Petrucci T.C. , Albertini A. M., Ranzani G. N., Bignami M., Mazzei F. (Functional analysis of MUTYH mutated proteins associated with familial adenomatous polyposis. DNA Repair. 9(6):700-7, 2010.

Molatore S., Russo M.T., D’Agostino V., Barone F., Matsumoto Y., Albertini A.M., Minoprio A., Degan P., Mazzei F., Bignami M. and Ranzani G.N. MUTYH mutations associated with familial adenomatous polyposis: functional characterizatio by a mammalian cell-based assay. Hum. Mut. 31: 159-166, 2010.

Serra I., Cecchini D.A., Ubiali D., Manazza E., Albertini A.M. and Terreni M. Coupling of site-directed mutagenesis and immobilization for the rational design of more efficient biocatalysts: the case of immobilized 3G3K PGA from E. coli. Eur. J. Org. Chem. 9:1384 -1389, 2009.

Marinoni I., Nonnis S., Monteferrante C., Heathcote P., Hartig E., Bottger L.H., Trautwein A.X., Negri A., Albertini A.M. and G. Tedeschi. Chracterization of L-aspartate oxidase and quinolinate synthase from Bacillus subtilis. FEBS Journal 275: 5090-5107, 2008.

Cecchini D. A., Serra I., Ubiali D., Terreni M., Albertini A.M. New active site oriented glyoxyl-agarose derivatives of Escherichia coli penicillin G acylase. BMC Biotechnology, 7: 54-58, 2007.

Hartig E., Hartmanz A., Schatzle M., Albertini A.M. and Jahn D. The Bacillus subtilis nrdEF genes, encoding a class Ib ribonucleotide reductase, are essential for aerobic and anaerobic growth. Appl Environ Microbiol. 72(8):5260-5, 2006.

Scaramozzino F., Estruch I., Rossolillo P. Terreni M. and Albertini A.M. Improvement of catalytic properties of Escherichia coli penicillin G acylase immobilized on glyoxyl agarose by addition of a six-amino-acid tag. Appl Environ. Microbiol. 71(12):8937-40, 2005.

Rossolillo P., Marinoni I., Galli E., Colosimo A. and Albertini A.M. YrxA is the transcriptional regulator that represses de novo NAD biosynthesis in Bacillus subtilis. J Bacteriol. 187(20):7155-60, 2005.

Ubiali D., Rocchietti S. , Scaramozzino F. , Terreni M. , Albertini A. M., Fernández-Lafuente R. , Guisán J. M., Pregnolato M. Synthesis of 2 -Deoxynucleosides by Transglycosylation with New Immobilized and Stabilized Uridine Phosphorylase and Purine Nucleoside Phosphorylase. Advanced Synthesis & Catalysis. 346 (11): 1361-1366, 2004.

Rocchietti S., Ubiali D., Terreni M., Albertini A.M., Fernandez-Lafuente R., Guisan J.M., Pregnolato M. Immobilization and stabilization of recombinant multimeric uridine and purine nucleoside phosphorylases from Bacillus subtilis. Biomacromolecules. 5(6):2195-2200, 2004.

Westers H., Dorenbos R., Van Dijl J.M., Kabel J., Flanagan T., Devine K.M., Jude .F, Seror S.J., Beekman A.C., Darmon E., Eschevins C., De Jong A., Bron S., Kuipers O.P., Albertini A.M., Antelmann H., Hecker M., Zamboni N., Sauer U., Bruand C., Ehrlich D.S., Alonso J.C., Salas M., Quax W.J. Genome Engineering Reveals Large Dispensable Regions in Bacillus subtilis. Mol Biol Evol. 20: 2076-2090, 2003

Kobayashi K., Ehrlich S.D., Albertini A., Amati G., Andersen K.K., Arnaud M., Asai K, Ashikaga S., Aymerich S, Bessieres P, Boland F, Brignell SC, Bron S, Bunai K, Chapuis J, Christiansen LC, Danchin A. et al.. Essential Bacillus subtilis genes. Proc. Natl. Acad. Sci. PNAS U S A. 100(8): 4678-83, 2003
Project Title:
Creation of hybrid strains in Bacillus by means of evolution engineering via protoplast fusion and genome shuffling.