Hybrid proteins containing proteorhodopsin from Exiguobacterium sibiricum

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Аннотация

The genes of hybrid proteins including Exiguobacterium sibiricum proteorhodopsin (ESR) and various N-terminal soluble domains have been constructed. Effective synthesis in Escherichia coli cells was observed only in the case of hybrids with chaperone Caf1M and maltose-binding protein MBP expressed as precursors with their own signal sequences. The study of the isolated MBP-ESR protein in micelles and proteoliposomes demonstrated formation and decay of the main photocycle intermediates at pH > 8. The photoelectric response of the hybrid proteins Caf-ESR and MBP-ESR is comparable in amplitude to the wild-type ESR response, indicating their homogeneous orientation in the membrane. The obtained constructions can be used to create bacterial expression systems for various retinal proteins, ensuring their uniform incorporation into proteoliposomes.

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Авторлар туралы

L. Petrovskaya

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, RAS; Moscow Institute of Physics and Technology

Хат алмасуға жауапты Автор.
Email: lpetr65@yahoo.com
Ресей, ul. Miklukho-Maklaya 16/10, Moscow, 117997; Institutskiy per. 9, Dolgoprudny, Moscow Region, 141701

E. Kryukova

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, RAS; Emanuel Institute of Biochemical Physics

Email: lpetr65@yahoo.com
Ресей, ul. Miklukho-Maklaya 16/10, Moscow, 117997; ul. Kosygina 4, Moscow, 119334

V. Bolshakov

Lomonosov Moscow State University

Email: lpetr65@yahoo.com

Faculty of Biology

Ресей, Leninskie gory 1/11, Moscow, 119234

E. Lukashev

Lomonosov Moscow State University

Email: lpetr65@yahoo.com

Faculty of Biology

Ресей, Leninskie gory 1/11, Moscow, 119234

S. Siletsky

Lomonosov Moscow State University

Email: lpetr65@yahoo.com

Belozersky Institute of Physico-Chemical Biology

Ресей, Leninskye gory 1/40, Moscow, 119992

M. Mamedov

Lomonosov Moscow State University

Email: lpetr65@yahoo.com

Belozersky Institute of Physico-Chemical Biology

Ресей, Leninskye gory 1/40, Moscow, 119992

R. Sudakov

Lomonosov Moscow State University

Email: lpetr65@yahoo.com

Belozersky Institute of Physico-Chemical Biology

Ресей, Leninskye gory 1/40, Moscow, 119992

D. Dolgikh

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, RAS; Emanuel Institute of Biochemical Physics; Lomonosov Moscow State University

Email: lpetr65@yahoo.com

Faculty of Biology, Lomonosov Moscow State University

Ресей, ul. Miklukho-Maklaya 16/10, Moscow, 117997; ul. Kosygina 4, Moscow, 119334; Leninskie gory 1/11, Moscow, 119234

M. Kirpichnikov

Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, RAS; Lomonosov Moscow State University

Email: lpetr65@yahoo.com

Faculty of Biology, Lomonosov Moscow State University

Ресей, ul. Miklukho-Maklaya 16/10, Moscow, 117997; Leninskie gory 1/11, Moscow, 119234

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2. Fig. 1. Schemes of the structure of hybrid proteins. SP is the signal sequence. The glycine-serine linker is shown in dark gray, and the hexahistidine sequence is shown in black.

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3. Fig. 2. Expression of ESR-containing fusion proteins in E. coli cells. Protein electrophoresis in 13% SDS-PAGE (a) and Western blot analysis (b) with anti-His-conjugate of membrane fraction samples from E. coli C43(DE3) cells expressing fusion proteins (lanes 1–7) and wild-type ESR (lane 8). Lanes 1–7 correspond to the numbering of the constructs in Fig. 1. M – protein molecular weight markers (kDa).

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4. Fig. 3. MBP-ESR photocycle in DDM micelles at pH 7 (a) and pH 9 (b).

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5. Fig. 4. Kinetics of transmembrane potential difference (ΔΨ) formation by proteoliposomes containing wild-type ESR and fusion proteins at pH 7.5. The arrow marks the moment of laser flash. Data for ESR, Caf-ESR, ESR-Cherry and ESR-Trx are taken from the article by Petrovskaya et al. [37].

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6. Fig. 5. Kinetics of light-induced changes in absorption at characteristic wavelengths by proteoliposomes containing MBP-ESR at pH 7.5 (a) and 8.5 (b).

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