Białka uczestniczące w transporcie jonów żelaza(II) w bakteriach gram-ujemnych

• Autorzy: Kierpiec Karolina , Stokowa-Sołtys Kamila

Warianty tytułu

EN

Proteins involved in the ferrous ions transport in gram-negative bacteria

• Języki publikacji: PL

Abstrakty

EN

Continuous increase in the number of multidrug-resistant strains forces us to look for drugs with completely new mode of action. One of the bacterial property determining the pathogenicity of these microorganisms is their ability to obtain iron. Because in the living environment of these single-celled individuals, its concentration is much lower than this necessary for their growth. For this reason, bacteria created various type of iron aquisition systems, including the Feo system, which mechanism of Fe²⁺ ion uptake is not fully understood, and protein from the Hmu family belonging to ABC transporters. The Feo transport system is one of the most common systems that is exclusively responsible for importing Fe²⁺ ions. It consists of three proteins: FeoA, FeoB and FeoC. FeoB is a transmembrane protein that is believed to play a key role in the mechanism of Fe²⁺ ion uptake. The other two components are cytoplasmic proteins. Both, FeoA and FeoC, are cytoplasmic proteins resembling the construction of transcription regulators. ABC transporters play an equally important role in maintaining iron homeostasis. These include proteins from Hmu family. HmuUV complex catalyses the import of these ions in hem iron form. The structure of this complex consists of TMD dimer (HmuU) and NBD dimer (HmuV). The HmuU is considered to be a permease - just like the FeoB described earlier while HmuV is the ATP binding protein.

Słowa kluczowe

PL

transport jonów żelaza(II); bakterie gram-ujemne; Feo; ferrous iron transport; Hmu; hemin uptake protein

EN

ferrous ions transport; gram-negative bacteria; Feo; ferrous iron transport; Hmu; hemin uptake protein

• Wydawca: Polskie Towarzystwo Chemiczne
• Czasopismo: Wiadomości Chemiczne
• Rocznik: 2021
• Tom: [Z] 75, 3-4
• Strony: 375--394
• Opis fizyczny: Bibliogr. 41 poz., rys.

Twórcy

autor

Kierpiec Karolina

• Wydział Chemii Uniwersytetu Wrocławskiego, ul. Joliot-Curie 14, 50-383 Wrocław

• https://orcid.org/0000-0001-9128-6750

autor

Stokowa-Sołtys Kamila

• Wydział Chemii Uniwersytetu Wrocławskiego, ul. Joliot-Curie 14, 50-383 Wrocław

• https://orcid.org/0000-0003-4723-0658

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Uwagi

Opracowanie rekordu ze środków MNiSW, umowa Nr 461252 w ramach programu "Społeczna odpowiedzialność nauki" - moduł: Popularyzacja nauki i promocja sportu (2021).