ΕΚΠΑ Βιοπληροφορική: Διδάσκοντες / Ευάγγελος Μουδριανάκης

ΔΙΔΑΚΤΙΚΟ ΠΡΟΣΩΠΙΚΟ | ΒΟΗΘΟΙ ΔΙΔΑΣΚΑΛΙΑΣ

Οι υπεύθυνοι για τη διδασκαλία των μαθημάτων του Προγράμματος προέρχονται από διάφορα Ανώτατα Εκπαιδευτικά Ιδρύματα, και συμμετέχουν ενεργά σε ερευνητικές δραστηριότητες.

Βιογραφικά σημειώματα:

Πληροφορίες για τον κάθε διδάσκοντα, την τρέχουσα ερευνητική του δραστηριότητα και τις δημοσιεύσεις του μπορείτε να δείτε ακολουθώντας τους συνδέσμους αριστερά, η επιλέγοντας από τον πιο κάτω πίνακα.

Περισσότερες πληροφορίες δίνονται παρακάτω:

Βιογραφικά σημειώματα: ΕΥΑΓΓΕΛΟΣ ΜΟΥΔΡΙΑΝΑΚΗΣ

Όνομα	ΕΥΑΓΓΕΛΟΣ ΜΟΥΔΡΙΑΝΑΚΗΣ
Θέση στο Έργο	Διδάσκων
Θέση στο Ίδρυμα	Καθηγητής Τμήματος Βιολογίας, ΕΚΠΑ
Προπτυχιακοί τίτλοι σπουδών	Πτυχίο Βιολογίας, Πανεπιστήμιο Αθηνών
Μεταπτυχιακοί τίτλοι σπουδών	Διδακτορικό στη Μοριακή Βιολογία Παν/μιο Johns Hopkins Μεταδιδακτορικές σπουδές Παν/μιο Johns Hopkins
Ερευνητικά Ενδιαφέροντα	"Assembly and Dynamics of Nucleoproteins and Chromosomes" Chromosome - Chromatin: The assembly, architecture and the control of transcription of the eukaryotic genetic apparatus are analyzed by cytological, biochemical and biophysical techniques ranging from in vitro cell culture and light and electron microscopy, through analytical ultracentrifugation and gel permeation chromatography, to x-ray crystallography and microcalorimetry. We have established that the histone "core" of the nucleosome is organized as a tripartite protein entity by the assembly of two dimers of H2A-H2B, one on each side of a centrally located H3-H4 tetramer. The contact interfaces of this assembly are considered as regulatory domains in the functional transitions of chromatin and are being probed by chemical, enzymatic and biophysical probes. We determined the crystal structure of the histone octamer to ca. 3? resolution and the arrangement of its subunits have revealed novel modes for polypeptide assembly (i.e., histone fold, handshake motif) and protein-DNA recognition and binding (i.e., paired element motifs PEMs). The path of the double helix over the histone octamer has been determined and found to be guided by the 12 repetitive PEMs. Using these geometric constraints, a high resolution model for the nucleosome has been obtained and optimized through molecular dynamics simulations in collaboration with Drs. C. S. Tung and A. E. Garcia of Los Alamos. These simulations revealed that the nucleosome fluctuations are dominated by motions in the DNA backbone. The nucleosome is surrounded by a positive ion cloud with an average local density exceeding by a factor of 5-10 the bulk phase ion concentration. We also see high water density at the protein-DNA boundaries, at the DNA grooves and especially between the two apposing gyres of the nucleosomal DNA. The energetics of the assembly of the nucleosomal components are analyzed microcalorimetrically through collaboration with Dr. E. Freire of the Biocalorimetry Center of this department. The patterns and specificity of protein-DNA interactions are analyzed by chemical, topological and structural methods. Nucleosome reconstitution experiments utilizing core histone subunits (regular and acetylated), transcription factors and specific sequences of circular DNA are in progress. "Bioenergetics" The mechanism of protein thermostability and enzyme thermoactivity in Archaea are studied. Particular emphasis is focused on the role of osmolytes in protein stabilization.

Επιλεγμένες Δημοσιεύσεις

Eickbush, T.H., and Moudrianakis, E.N., 1978. The Histone Core Complex: An Octamer Assembled by Two Sets of Protein-Protein Interactions. Biochemistry, 17, 4955-4964.

Moudrianakis, E.N., and Horner, R.D., 1990. The PKa-Gate Mechanism for Protonmotive Coupling. In Molecular Structure, Function and Assembly of the ATP Synthetases., pp. 181-193. Edited by S. Marzuki, Plenum Press, New York.

Arents, G., Burlingame, R. W., Wang, B-C., Love, W. E, and Moudrianakis, E. N. 1991. The nucleosomal core histone octamer at 3.1 ? resolution: A tripartite protein assembly and a left-handed superhelix. Proc. Natl. Acad. Sci. USA 88, 10148-10152.

Moudrianakis, E. N. and Arents, G. 1993. Structure of the histone octamer core of the nucleosome and its potential interactions with DNA. Cold Spring Harbor Symposia on Quantitative Biology, Volume LVIII, 273-279.

Baxevanis, A. D., Arents, G., Moudrianakis, E. N., and Landsman, D. 1995. A variety of DNA-Binding and Multimeric Proteins Contain the Histone Fold Motif. Nucleic Acid Research, 24, 2685-2691.

Arents, G., and Moudrianakis, E. N., 1995. The Histone Fold: A Ubiquitous Architectural Motif Utilized in DNA Compaction and Protein Dimerization. Proc. Natl. Acad. Sci. USA, 92, 11170-11174.

Kruger, W., Peterson, C. L., Sil, A., Coburn, C., Arents, G., Moudrianakis, E. N., and Herskowitz, I., 1995. Amino Acid Substitutions in the Structured Domains of Histones H3 and H4 Partially Relieve the Requirement of the Yeast SWI/SNF Complex for Transcription. Genes & Development, 9, 2770-2779.

Karantza, V., Freire, E., and Moudrianakis, E. N., 1996. Thermodynamic Studies of the Core Histones: pH and Ionic Strength Effects on the Stability of the (H3-H4)/(H3-H4)2 System. Biochemistry, 35, 2037-2046.

Pruss, D., Bartholomew, B., Persinger, J., Hayes, J., Arents, G., Moudrianakis, E.N., and Wolffe, A.P. 1996. An Asymmetric Model for the Nucleosome: A Binding Site for Linker Histones Inside the DNA Gyres, Science, 274, 614-617.

Santisteban, M.S., Arents, G., Moudrianakis, E.N., and Smith, M., 1997. Histone Octamer Function in vivo: Mutations in the Dimer-Tetramer Interfaces Disrupt Both Gene Activation and Repression, EMBO Journal, 16, 2493-2506.

Bal, Wojciech, Karantza, V., Moudrianakis, E. N., and Kasprzak, K. 1999. Interation of Nickel (II) with Histones: In vitro Binding of Nickel (II) to the Core Histone Tetramer. Archives of Biochem. and Biophys. 364, 161-166.

Karantza, V., Freire, E., and Moudrianakis, E. N., 2001. Thermodynamic studies of the core histones: stability of the octamer subunits is not altered by removal of their terminal domains. Biochemistry 43, 13114-23.

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