NapB Restores cytochrome c biosynthesis in bacterial dsbD-deficient mutants

Guo, Kailun; Xue, Feng; Sun, Weining; Han, Sirui; Wu, Shihua; Gao, Haichun

doi:10.1038/s42003-022-03034-3

Cited by 10 publications

(3 citation statements)

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“…1D ). As CyaA/CyaC and CpdA catalyze synthesis and degradation of cAMP, respectively, and cAMP at elevated concentrations enhances the cyt c abundance in S. oneidensis ( 31 ), these insertions are fully justified ( 32 , 33 ).…”

Section: Resultsmentioning

confidence: 99%

Bacterial TANGO2 homologs are heme-trafficking proteins that facilitate biosynthesis of cytochromes c

Han

Guo

Wang

et al. 2023

mBio

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Heme, an essential molecule for virtually all living organisms, acts primarily as a cofactor in a large number of proteins. However, how heme is mobilized from the site of synthesis to the locations where hemoproteins are assembled remains largely unknown in cells, especially bacterial ones. In this study, with Shewanella oneidensis as the model, we identified HtpA (SO0126) as a heme-trafficking protein and homolog of TANGO2 proteins found in eukaryotes. We showed that HtpA homologs are widely distributed in all domains of living organisms and have undergone parallel evolution. In its absence, the cytochrome (cyt) c content and catalase activity decreased significantly. We further showed that both HtpA and representative TANGO2 proteins bind heme with 1:1 stoichiometry and a relatively low dissociation constant. Protein interaction analyses substantiated that HtpA directly interacts with the cytochrome c maturation system. Our findings shed light on cross-membrane transport of heme in bacteria and extend the understanding of TANGO2 proteins. IMPORTANCE The intracellular trafficking of heme, an essential cofactor for hemoproteins, remains underexplored even in eukaryotes, let alone bacteria. Here we developed a high-throughput method by which HtpA, a homolog of eukaryotic TANGO2 proteins, was identified to be a heme-binding protein that enhances cytochrome c biosynthesis and catalase activity in Shewanella oneidensis . HtpA interacts with the cytochrome c biosynthesis system directly, supporting that this protein, like TANGO2, functions in intracellular heme trafficking. HtpA homologs are widely distributed, but a large majority of them were found to be non-exchangeable, likely a result of parallel evolution. By substantiating the heme-trafficking nature of HtpA and its eukaryotic homologs, our findings provide general insight into the heme-trafficking process and highlight the functional conservation along evolution in all living organisms.

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Section: Resultsmentioning

confidence: 99%

Bacterial TANGO2 homologs are heme-trafficking proteins that facilitate biosynthesis of cytochromes c

Han

Guo

Wang

et al. 2023

mBio

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“…Since the physiological stimulus for BarA has been suggested to be metabolic end products 39,42,69,70 , we speculate that perhaps shifts in carbon metabolism or some secondary metabolite processes trigger the response, thereby putting siderophore biosynthesis under the control of cellular metabolic status. Coupling carbon metabolism and iron uptake may be particularly important for Shewanella as this group of bacteria encodes a vast number of iron-containing proteins, many of which are involved in metabolism as enzymes and electron carriers 71,72 .…”

Section: Discussionmentioning

confidence: 99%

Multifaceted regulation of siderophore synthesis by multiple regulatory systems in Shewanella oneidensis

Xie,

Xu,

Tang

et al. 2024

Commun Biol

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Siderophore-dependent iron uptake is a mechanism by which microorganisms scavenge and utilize iron for their survival, growth, and many specialized activities, such as pathogenicity. The siderophore biosynthetic system PubABC in Shewanella can synthesize a series of distinct siderophores, yet how it is regulated in response to iron availability remains largely unexplored. Here, by whole genome screening we identify TCS components histidine kinase (HK) BarA and response regulator (RR) SsoR as positive regulators of siderophore biosynthesis. While BarA partners with UvrY to mediate expression of pubABC post-transcriptionally via the Csr regulatory cascade, SsoR is an atypical orphan RR of the OmpR/PhoB subfamily that activates transcription in a phosphorylation-independent manner. By combining structural analysis and molecular dynamics simulations, we observe conformational changes in OmpR/PhoB-like RRs that illustrate the impact of phosphorylation on dynamic properties, and that SsoR is locked in the ‘phosphorylated’ state found in phosphorylation-dependent counterparts of the same subfamily. Furthermore, we show that iron homeostasis global regulator Fur, in addition to mediating transcription of its own regulon, acts as the sensor of iron starvation to increase SsoR production when needed. Overall, this study delineates an intricate, multi-tiered transcriptional and post-transcriptional regulatory network that governs siderophore biosynthesis.

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“…KDM3A plays a role in regulating the expression of extracellular matrix and fat metabolic genes during ferroptosis. [8] Therefore, it is of interest to examine the role of KDM3A in the regulation of the extracellular matrix and fat metabolic gene expression using next-generation knowledge discovery (NGKD) methods. Microarray data were obtained from the Gene Expression Omnibus (GEO) database (accession number GSE120739).…”

Section: Introductionmentioning

confidence: 99%

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2024

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The author's state that they adhere with COPE guidelines on publishing ethics as described elsewhere at https://publicationethics.org/. The authors also undertake that they are not associated with any other third party (governmental or non-governmental agencies) linking with any form of unethical issues connecting to this publication. The authors also declare that they are not withholding any information that is misleading to the publisher in regard to this article.

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NapB Restores cytochrome c biosynthesis in bacterial dsbD-deficient mutants

Cited by 10 publications

References 75 publications

Bacterial TANGO2 homologs are heme-trafficking proteins that facilitate biosynthesis of cytochromes c

Bacterial TANGO2 homologs are heme-trafficking proteins that facilitate biosynthesis of cytochromes c

Multifaceted regulation of siderophore synthesis by multiple regulatory systems in Shewanella oneidensis

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