The YcnI protein from Bacillus subtilis contains a copper-binding domain

Abstract

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Post-transcriptional regulation by copper with a new upstream Open Reading Frame

“…Among those TBDTs are OprC-type transporters (signature TIGR01778), one of which was recently shown to be specific for Cu (Bhamidimarri et al, 2021). Other genes frequently found in operons with bp2923 homologues code for proteins involved in Cu transport, binding or homeostasis, including the chaperones ScoC and Pcu A C that participate in the assembly of heme-copper subunits of respiratory complexes (Serventi et al, 2012, Trasnea et al, 2016), and the Cu-binding proteins YcnI and CopC (Damle et al, 2021, Lawton et al, 2016). Some of these operons also comprise MbnPH-like genes notably found in biosynthetic operons of Cu-binding methanobactin-type molecules (Kenney and Rosenzweig, 2018, Manesis et al, 2021), and AhpC_TSA genes, whose products detoxify peroxides (Dubbs and Mongkolsuk, 2007).…”

Copper delivery to an endospore coat protein of Bacillus subtilis

“…(A) An overview of Cu homeostasis in B. subtilis including Cu (orange circles, oxidation state undefined) export by CopA and CopZ (regulated by CsoR) ( Smaldone and Helmann 2007 ), and import by YcnJ (regulated by YcnK) ( Chillappagari et al, 2009 ; Hirooka et al, 2012 ). YcnI is membrane bound and binds Cu(II) in vitro , but its role in Cu homeostasis is unclear ( Damle et al, 2021 ). The only currently known Cu-requiring enzymes in vegetative B. subtilis cells are two cytochrome oxidases (COXs) located on the plasma membrane ( Lauraeus et al, 1991 ).…”

Intracellular copper storage and delivery in a bacterium

“…(20,22). YcnI is also membrane bound and binds Cu(II) in vitro, but its role in Cu homeostasis is unclear (23). The only currently known Cu-requiring enzymes in vegetative B. subtilis cells are two cytochrome oxidases (COXs) located on the plasma membrane (11,24).…”

“…The Gram-positive bacterium Bacillus subtilis is an excellent model system for investigating the role of a Csp3, as its Cu homeostasis system is well characterised (Figure 1a) (7,(18)(19)(20)(21)(22)(23).…”

“…The membrane-anchored YcnI is part of the same (ycnKJI) operon and is also regulated by YcnK (22). The soluble domain of YcnI binds Cu(II) in vitro, and this protein has been suggested to function as a Cu metallochaperone (23).…”