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Effect of chaperonin encoded by gene 146 on thermal aggregation of lytic proteins of bacteriophage EL Pseudomonas aeruginosa

Authors
  • Semenyuk, P. I.1
  • Orlov, V. N.1
  • Kurochkina, L. P.1, 2
  • 1 Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119234, Russia , Moscow (Russia)
  • 2 Russian Academy of Sciences, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow, 117997, Russia , Moscow (Russia)
Type
Published Article
Journal
Biochemistry (Moscow)
Publisher
Pleiades Publishing
Publication Date
Feb 18, 2015
Volume
80
Issue
2
Pages
172–179
Identifiers
DOI: 10.1134/S0006297915020042
Source
Springer Nature
Keywords
License
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Abstract

Investigation of the chaperonin encoded by gene 146 of bacteriophage EL Pseudomonas aeruginosa that we characterized earlier has been continued. To reveal the mechanism of its functioning, new recombinant substrate proteins, fragments of gene product (gp) 183 containing the lysozyme domain were prepared. Their interaction with gp146 was studied. The influence of the phage chaperonin on the thermal aggregation of one of these gp183 fragments and endolysin (gp188) was investigated in both the presence and the absence of ATP by dynamic light scattering. In the absence of ATP, the phage chaperonin forms stable complexes with substrate proteins, thereby protecting them against thermal aggregation. Experimental data obtained for different substrate proteins are analyzed.

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