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Titolo:
Building a replisome solution structure by elucidation of protein-protein interactions in the bacteriophage T4 DNA polymerise holoenzyme
Autore:
Alley, SC; Trakselis, MA; Mayer, MU; Ishmael, FT; Jones, AD; Benkovic, SJ;
Indirizzi:
Penn State Univ, Dept Chem, University Pk, PA 16802 USA Penn State Univ University Pk PA USA 16802 m, University Pk, PA 16802 USA Penn State Univ, Dept Biochem & Mol Biol, Hershey Med Ctr, University Pk, PA 16802 USA Penn State Univ University Pk PA USA 16802 r, University Pk, PA 16802 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 42, volume: 276, anno: 2001,
pagine: 39340 - 39349
SICI:
0021-9258(20011019)276:42<39340:BARSSB>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL NUCLEAR ANTIGEN; C-TERMINAL REGION; SLIDING CLAMP; REPLICATION FORK; PROCESSIVITY FACTOR; CRYSTAL-STRUCTURE; CARBOXYL-TERMINUS; CATALYTIC SUBUNIT; III HOLOENZYME; COMPLEX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Benkovic, SJ Penn State Univ, Dept Chem, 414 Wartik Lab, University Pk, PA16802 USA Penn State Univ 414 Wartik Lab University Pk PA USA 16802 USA
Citazione:
S.C. Alley et al., "Building a replisome solution structure by elucidation of protein-protein interactions in the bacteriophage T4 DNA polymerise holoenzyme", J BIOL CHEM, 276(42), 2001, pp. 39340-39349

Abstract

Assembly of DNA replication systems requires the coordinated actions of many proteins. The multiprotein complexes formed as intermediates on the pathway to the final DNA polymerase holoenzyme have been shown to have distinctstructures relative to the ground-state structures of the individual proteins. By using a variety of solution-phase techniques, we have elucidated additional information about the solution structure of the bacteriophage T4 holoenzyme. Photocross-linking and mass spectrometry were used to demonstrate interactions between I107C of the sliding clamp and the DNA polymerase. Fluorescence resonance energy transfer, analytical ultracentrifugation, and isothermal titration calorimetry measurements were used to demonstrate thatthe C terminus of the DNA polymerase can interact at two distinct locations on the sliding clamp. Both of these binding modes may be used during holoenzyme assembly, but only one of these binding modes is found in the final holoenzyme. Present and previous solution interaction data were used to build a model of the holoenzyme that is consistent with these data.

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Documento generato il 29/09/20 alle ore 00:21:05