ChlR Protein of Synechococcus sp. PCC 7002 Is a Transcription Activator That Uses an Oxygen-sensitive [4Fe-4S] Cluster to Control Genes involved in Pigment Biosynthesis

Ludwig, Marcus; Pandelia, Maria-Eirini; Chew, Chyue Yie; Zhang, Bo; Golbeck, John H.; Krebs, Carsten; Bryant, Donald A.

doi:10.1074/jbc.m114.561233

Cited by 20 publications

(20 citation statements)

References 54 publications

(61 reference statements)

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“…When the deletion was complemented by inserting desE under its native promoter in the acsA locus (a location used previously for making chromosomal insertions [15]), 1,14-nonadecadiene production was restored. These results sug- (24), conditions that were not tested here. Precursors for 1,14-nonadecadiene biosynthesis.…”

Section: Resultsmentioning

confidence: 74%

A Desaturase Gene Involved in the Formation of 1,14-Nonadecadiene in Synechococcus sp. Strain PCC 7002

Mendez-Perez

Herman

Pfleger

2014

Appl Environ Microbiol

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The marine cyanobacterium Synechococcus sp. strain PCC 7002 synthesizes two alkenes, 1-nonadecene and 1,14-nonadecadiene. Whereas the genetic basis for the biosynthesis of the terminal double bond in both alkenes has been characterized, the origin of the internal double bond in 1,14-nonadecadiene has not. In this study, we demonstrate that a gene encoding an uncharacterized desaturase is involved in the formation of the internal double bond of 1,14-nonadecadiene. Further, at low temperatures, the desaturase gene is essential for growth, and in wild-type cells the levels of 1,14-nonadecadiene increase relative to that of cells grown at 38°C. These data suggest that 1,14-nonadecadiene plays a role in responding to cold stress.

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Section: Resultsmentioning

confidence: 74%

A Desaturase Gene Involved in the Formation of 1,14-Nonadecadiene in Synechococcus sp. Strain PCC 7002

Mendez-Perez

Herman

Pfleger

2014

Appl Environ Microbiol

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“…Phycocyanobilin and phycoerthrobilin are the most common chromophores (16,363). Cyanobacteria typically have two forms of heme oxygenase, one of which is produced constitutively (Hox1) and another that is synthesized under microoxic conditions (Hox2) (364). In plants, algae, and cyanobacteria, various bilins are produced from biliverdin by enzymes known as ferredoxin-dependent bilin reductases (FDBR) (for a review, see (17)).…”

Section: Phycobiliproteinsmentioning

confidence: 99%

Biosynthesis of the modified tetrapyrroles—the pigments of life

Bryant

Hunter

Warren

2020

Journal of Biological Chemistry

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199

164

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Modified tetrapyrroles are large macrocyclic compounds, consisting of diverse conjugation and metal chelation systems and imparting an array of colors to the biological structures that contain them. Tetrapyrroles represent some of the most complex small molecules synthesized by cells and are involved in many essential processes that are fundamental to life on Earth, including photosynthesis, respiration, and catalysis. These molecules are all derived from a common template through a series of enzyme-mediated transformations that alter the oxidation state of the macrocycle and also modify its size, its side-chain composition, and the nature of the centrally chelated metal ion. The different modified tetrapyrroles include chlorophylls, hemes, siroheme, corrins (including vitamin B12), coenzyme F430, heme d1, and bilins. After nearly a century of study, almost all of the more than 90 different enzymes that synthesize this family of compounds are now known, and expression of reconstructed operons in heterologous hosts has confirmed that most pathways are complete. Aside from the highly diverse nature of the chemical reactions catalyzed, an interesting aspect of comparative biochemistry is to see how different enzymes and even entire pathways have evolved to perform alternative chemical reactions to produce the same end products in the presence and absence of oxygen. Although there is still much to learn, our current understanding of tetrapyrrole biogenesis represents a remarkable biochemical milestone that is summarized in this review.

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“…centers in proteins such as aconitase and fumarate and in nitrate reduction transcriptional regulator (FNR) (26,27). We next analyzed TtuA treated with excess ferricyanide.…”

Section: +mentioning

confidence: 99%

Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by an iron-sulfur protein TtuA

Chen

Asai

Narai

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Two-thiouridine (s 2 U) at position 54 of transfer RNA (tRNA) is a posttranscriptional modification that enables thermophilic bacteria to survive in high-temperature environments. s 2 U is produced by the combined action of two proteins, 2-thiouridine synthetase TtuA and 2-thiouridine synthesis sulfur carrier protein TtuB, which act as a sulfur (S) transfer enzyme and a ubiquitin-like S donor, respectively. Despite the accumulation of biochemical data in vivo, the enzymatic activity by TtuA/TtuB has rarely been observed in vitro, which has hindered examination of the molecular mechanism of S transfer. Here we demonstrate by spectroscopic, biochemical, and crystal structure analyses that TtuA requires oxygen-labile [4Fe-4S]-type iron (Fe)-S clusters for its enzymatic activity, which explains the previously observed inactivation of this enzyme in vitro. The [4Fe-4S] cluster was coordinated by three highly conserved cysteine residues, and one of the Fe atoms was exposed to the active site. Furthermore, the crystal structure of the TtuA-TtuB complex was determined at a resolution of 2.5 Å, which clearly shows the S transfer of TtuB to tRNA using its C-terminal thiocarboxylate group. The active site of TtuA is connected to the outside by two channels, one occupied by TtuB and the other used for tRNA binding. Based on these observations, we propose a molecular mechanism of S transfer by TtuA using the ubiquitin-like S donor and the [4Fe-4S] cluster.Fe-S cluster | sulfur transfer | tRNA modification | 2-thiouridine | crystal structure

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ChlR Protein of Synechococcus sp. PCC 7002 Is a Transcription Activator That Uses an Oxygen-sensitive [4Fe-4S] Cluster to Control Genes involved in Pigment Biosynthesis

Abstract: Background: A four-gene operon, acsF

Cited by 20 publications

References 54 publications

A Desaturase Gene Involved in the Formation of 1,14-Nonadecadiene in Synechococcus sp. Strain PCC 7002

A Desaturase Gene Involved in the Formation of 1,14-Nonadecadiene in Synechococcus sp. Strain PCC 7002

Biosynthesis of the modified tetrapyrroles—the pigments of life

Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by an iron-sulfur protein TtuA

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