Dynamic light scattering study of base excision DNA repair proteins and their complexes

Inna A. Vasil'eva, Rashid O. Anarbaev, Nina A. Moor, Olga I. Lavrik

Результат исследования: Научные публикации в периодических изданияхстатья

8 Цитирования (Scopus)

Аннотация

Base excision repair (BER) involves many enzymes acting in a coordinated fashion at the most common types of DNA damage. The coordination is facilitated by interactions between the enzymes and accessory proteins, X-ray repair cross-complementing protein 1 (XRCC1) and poly(ADP-ribose) polymerase 1 (PARP1). Here we use dynamic light scattering (DLS) technique to determine the hydrodynamic sizes of several BER enzymes and proteins, DNA polymerase β (Polβ), apurinic/apyrimidinic endonuclease 1 (APE1), tyrosyl-DNA phosphodiesterase 1 (TDP1), XRCC1 and PARP1, present alone or in the equimolar mixtures with each other. From the DLS data combined with glutaraldehyde cross-linking experiments and previous quantitative binding data the oligomeric states of BER proteins and their complexes are estimated. All the proteins have been proposed to form homodimers upon their self-association. The most probable oligomerization state of the binary complexes formed by PARP1 with various proteins is a heterotetramer. The oligomerization state of the binary complexes formed by XRCC1 varies from heterodimer to heterotetramer, depending on the partner. The DLS technique is applied for the first time to measure the hydrodynamic sizes of PARP1 molecules covalently bound with poly(ADP-ribose) (PAR) synthesized upon the automodification reaction. PARP1 has been detected to form huge conglomerates stabilized by Mg2+ coordinated bonds with PAR polymers.

Язык оригиналаанглийский
Страницы (с-по)297-305
Число страниц9
ЖурналBiochimica et Biophysica Acta - Proteins and Proteomics
Том1867
Номер выпуска3
DOI
СостояниеОпубликовано - 1 мар 2019

Fingerprint Подробные сведения о темах исследования «Dynamic light scattering study of base excision DNA repair proteins and their complexes». Вместе они формируют уникальный семантический отпечаток (fingerprint).

  • Цитировать