Εξειδίκευση τύπου :	Περίληψη σε συνέδριο
Τίτλος:	Phosphate specific transporter system (PSTS) in Thermus thermophilus involves a DING phosphatase
Δημιουργός/Συγγραφέας:	Pantazaki, A. A. Tsolkas, G. P. [EL] Κυριακίδης, Δ.Α.[EN] Kyriakidis, D.A.
Εκδότης:	Springer
Ημερομηνία:	2007
Γλώσσα:	Αγγλικά
ISSN:	0939-4451
DOI:	10.1007/s00726-007-0578-0
Περίληψη:	Phosphate transport in bacteria occurs via a phosphate specific transporter system (PSTS) that belongs to the ABC family of transporters a multisubunit system containing an alkaline phosphatase. DING proteins were characterized due to the N-terminal amino acid sequence DINGGGATL which is highly conserved in animal and plant isolates but more variable in microbes. Most prokaryotic homologues of the DING proteins often have some structural homology to phosphatases or periplasmic phos- 10th International Congress on Amino Acids and Proteins LXIX phate-binding proteins. In E. coli the product of the inducible gene DinG possesses ATP hydrolyzing helicase enzymic activity. An alkaline phosphorolytic enzyme of the PSTS system was purified to homogeneity from the thermophilic bacterium Thermus thermophilus. N-terminal sequence analysis of this protein revealed the same high degree of similarity to DING proteins especially to the human synovial stimulatory protein P205 the steroidogenesis-inducing protein and to the phosphate ABC transporter periplasmic phosphate-binding protein putative [P. fluorescens Pf-5]. The enzyme had a molecular mass of 40 kDa on SDS=PAGE exhibiting optimal phosphatase activity at pH 12.3 and 70 _C. The enzyme possessed characteristics of a DING protein such as ATPase ds endonuclease and 30phosphodiesterase (30-exonuclease) activities and binding to linear dsDNA displaying helicase activity on supercoiled DNA. In this work the purification and biochemical characterization of a T. thermophilus DING protein was achieved. The biochemical properties N-terminal sequence similarities of this protein implied that the enzyme belongs to the PSTS family and might be involved in the DNA repair mechanism of this microorganism.
Όνομα εκδήλωσης:	10th International Congress on Amino Acids and Proteins (ICAAP)
Τίτλος πηγής δημοσίευσης:	Amino Acids
Τόμος/Κεφάλαιο:	33
Τεύχος:	3
Θεματική Κατηγορία:	[EL] Ανόργανη χημεία[EN] Inorganic chemistry [EL] Βιοχημεία[EN] Biochemistry [EL] Βιοτεχνολογία[EN] Biotechnology
Αξιολόγηση από ομότιμους (peer reviewed):	Ναι
Ηλεκτρονική διεύθυνση περιοδικού (link) :	http://www.springer.at/amino_acids
Σημειώσεις:	Abstract
Εμφανίζεται στις συλλογές:	Άλλες δράσεις