Evidence map›Paper›PMID 40690053›Full record

ArticleBioresources and bioprocessing2025

Using of transporter proteins to improve the uptake efficiency of hydrophobic compounds by Escherichia coli: a coordinated synthesis of START protein and P450scc system proteins to enhance cholesterol biotransformation.

Sofia V Zamalutdinova, Ludmila V Isaeva, Yaroslav V Faletrov, Nikolay N Eroshchenko, Alexey N Kirushin, Vadim N Tashlitsky, Mikhail A Rubtsov, Ludmila A Novikova

Abstract read
In one paragraph

Article in Bioresources and bioprocessing, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Sofia V ZamalutdinovaFaculty of Biology, M.V. Lomonosov Moscow State University, Leninskie Gory, 1/12, Moscow, 119991, Russia. zamalutdinova.sofya@mail.ru.ORCID http://orcid.org/0009-0006-9510-1868
Ludmila V IsaevaBelozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Leninskie Gory 1/40, Moscow, 119991, Russia.ORCID http://orcid.org/0009-0001-3638-0290
Yaroslav V FaletrovResearch Institute for Physical Chemical Problems, Belarusian State University, Minsk, 220030, Belarus.ORCID http://orcid.org/0000-0001-8168-5897
Nikolay N EroshchenkoI.M. Sechenov First Moscow State Medical University, Moscow, 119991, Russia.ORCID http://orcid.org/0000-0001-8677-1946
Alexey N KirushinI.M. Sechenov First Moscow State Medical University, Moscow, 119991, Russia.ORCID http://orcid.org/0000-0003-1799-0402
Vadim N TashlitskyFaculty of Chemistry, M.V. Lomonosov Moscow State University, Moscow, 119991, Russia.ORCID http://orcid.org/0000-0003-4100-2419
Mikhail A RubtsovFaculty of Biology, M.V. Lomonosov Moscow State University, Leninskie Gory, 1/12, Moscow, 119991, Russia.ORCID http://orcid.org/0000-0003-4947-1009
Ludmila A NovikovaBelozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Leninskie Gory 1/40, Moscow, 119991, Russia. novik@genebee.msu.ru.ORCID http://orcid.org/0009-0009-1563-5723

Funding

Russian Foundation for Fundamental Investigations 20-08-00467A
6 · The paper itself

Abstract

Synthesis of steroid drugs is possible through biotechnological methods, however, the low efficiency of transporting steroid substrates across microbial membranes is the challenge in using microorganisms for their production. STARD1 and STARD3 proteins (members of the START domain family) work in some mammalian cells in conjunction with the steroidogenic P450scc enzyme system (cytochrome P450scc, adrenodoxin reductase, and adrenodoxin), transporting cholesterol to the mitochondria, where cytochrome P450scc converts it into pregnenolone. In this study, we investigated the effect of STARD1 and STARD3 on P450scc efficiency in E. coli expression models. The combination of the STARD3(216-444) or STARD1(53-285) protein bearing an N-terminal periplasm-targeting sequence, with the P450scc system reconstituted in E. coli, resulted in an increase of pregnenolone synthesis by 3.2- and 1.9-fold, respectively, on a laboratory scale. STARD3(216-444) showed higher levels of expression and a greater effect on the incorporation of sterols into cells and whole-cell biotransformation of cholesterol, compared to STARD1(53-285). This study proposes a fundamentally new approach to optimizing the functioning of the P450scc system in microbial cells, which uses the cholesterol transfer protein to increase the uptake efficiency of a poorly soluble steroid substrate by bacteria. The demand for steroid medications is increasing, and the use of specific carrier proteins could be a useful tool to enhance the efficiency of whole-cell biosynthesis of various steroid compounds.

Identifiers

PMID40690053
PMCPMC12279672

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.