Molecular mechanisms of glycogen particle assembly in Escherichia coli

Li, Fen; Wang, Mengmeng; Liu, Qinghua; Ma, Zhang-Wen; Wang, Jun‐Jiao; Wang, Ziyi; Tang, Jia-Wei; Lyu, Jing-Wen; Zhu, Zuobin; Wang, Liang

doi:10.1016/j.carbpol.2022.120200

Cited by 2 publications

(3 citation statements)

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“…In sample C14, genes involved in sucrose metabolism were generally downregulated, which not only affected sugar utilization but also had an impact on glycogen metabolism. Previous studies have supported the idea that bacterial glycogen storage and overaccumulation could lead to better growth or a higher OD 600 value [ 16 ]. A study demonstrated that an E. coli mutant with a single gene disruption in glgBXCAP , a key gene cluster involved in glycogen metabolism, exhibited increased glycogen accumulation, which facilitated growth but reduced glucose consumption in liquid culture [ 17 ].…”

Section: Resultsmentioning

confidence: 93%

Regulation mechanism and bioactivity characteristic of surfactin homologues with C14 and C15 fatty acid chains

Su,

Gao,

et al. 2024

Microb Cell Fact

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Background Surfactin, a green lipopeptide bio-surfactant, exhibits excellent surface, hemolytic, antibacterial, and emulsifying activities. However, a lack of clear understanding of the synthesis regulation mechanism of surfactin homologue components has hindered the customized production of surfactin products with different biological activities. Results In this study, exogenous valine and 2-methylbutyric acid supplementation significantly facilitated the production of C14–C15 surfactin proportions (up to 75% or more), with a positive correlation between the homologue proportion and fortified concentration. Subsequently, the branched-chain amino acid degradation pathway and the glutamate synthesis pathway are identified as critical pathways in regulating C14–C15 surfactin synthesis by transcriptome analysis. Overexpression of genes bkdAB and glnA resulted in a 1.4-fold and 1.3-fold increase in C14 surfactin, respectively. Finally, the C14-rich surfactin was observed to significantly enhance emulsification activity, achieving an EI24 exceeding 60% against hexadecane, while simultaneously reducing hemolytic activity. Conversely, the C15-rich surfactin demonstrated an increase in both hemolytic and antibacterial activities. Conclusion This study presents the first evidence of a potential connection between surfactin homologue synthesis and the conversion of glutamate and glutamine, providing a theoretical basis for targeting the synthesis regulation and structure–activity relationships of surfactin and other lipopeptide compounds. Graphical Abstract

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Section: Resultsmentioning

confidence: 93%

Regulation mechanism and bioactivity characteristic of surfactin homologues with C14 and C15 fatty acid chains

Su,

Gao,

et al. 2024

Microb Cell Fact

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“…103 Recent studies in bacteria indicate that α-particles states are modulated by the association of enzymes, accounting for fragile and stable states due to changes in average chain length, allowing for the control of glycogen storage and degradation. 104 The internal structure and architecture of the glycogen particle were first conceptualized by the "tiered model" based on the molecular arrangement of the α-glucan presenting two chain types: unbranched A-chains and branched Bchains 105−107 (Figure 2E). Specifically, branches in B-chains are uniformly distributed, comprising two branches that generate further A-or B-chains.…”

Section: The Architecture Of α-Glucans In Bacteriamentioning

confidence: 99%

“…In animals, it has been observed that the small β-particles degrade more easily to glucose than α-particles . Recent studies in bacteria indicate that α-particles states are modulated by the association of enzymes, accounting for fragile and stable states due to changes in average chain length, allowing for the control of glycogen storage and degradation …”

Section: Architecture Of α-Glucansmentioning

confidence: 99%

Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes

Cifuente,

Colleoni,

Kalscheuer

et al. 2024

Chem. Rev.

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Bacteria have acquired sophisticated mechanisms for assembling and disassembling polysaccharides of different chemistry. α-D-Glucose homopolysaccharides, so-called α-glucans, are the most widespread polymers in nature being key components of microorganisms. Glycogen functions as an intracellular energy storage while some bacteria also produce extracellular assorted α-glucans. The classical bacterial glycogen metabolic pathway comprises the action of ADP-glucose pyrophosphorylase and glycogen synthase, whereas extracellular α-glucans are mostly related to peripheral enzymes dependent on sucrose. An alternative pathway of glycogen biosynthesis, operating via a maltose 1phosphate polymerizing enzyme, displays an essential wiring with the trehalose metabolism to interconvert disaccharides into polysaccharides. Furthermore, some bacteria show a connection of intracellular glycogen metabolism with the genesis of extracellular capsular α-glucans, revealing a relationship between the storage and structural function of these compounds. Altogether, the current picture shows that bacteria have evolved an intricate α-glucan metabolism that ultimately relies on the evolution of a specific enzymatic machinery. The structural landscape of these enzymes exposes a limited number of core catalytic folds handling many different chemical reactions. In this Review, we present a rationale to explain how the chemical diversity of α-glucans emerged from these systems, highlighting the underlying structural evolution of the enzymes driving α-glucan bacterial metabolism.

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Molecular mechanisms of glycogen particle assembly in Escherichia coli

Cited by 2 publications

References 36 publications

Regulation mechanism and bioactivity characteristic of surfactin homologues with C14 and C15 fatty acid chains

Regulation mechanism and bioactivity characteristic of surfactin homologues with C14 and C15 fatty acid chains

Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes

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