Interplay between MPIase, YidC, and PMF during Sec-independent insertion of membrane proteins

Endo, Yuta; Shimizu, Yuko; Nishikawa, Hanako; Sawasato, Katsuhiro; Nishiyama, Kenichi

doi:10.26508/lsa.202101162

Cited by 20 publications

(19 citation statements)

References 34 publications

(68 reference statements)

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“…MPIase was required for insertion of both substrates. In the case of Pf3-Lep, the dependency on YidC/ PMF increased with increasing substrate level, whereas V15D insertion was promoted by YidC/PMF regardless of the substrate level (Endo et al, 2022). These results indicate that the number of negative charges on the N-terminal side and the substrate level strongly affect the dependency on YidC and PMF.…”

Section: Interaction Between Membrane Protein Integrase and Yidcmentioning

confidence: 80%

“…The interplay of MPIase with YidC and PMF in the Secindependent pathway has also been analyzed using different substrates (Endo et al, 2022). In vivo experiments have shown that Pf3-Lep, an N-out type substrate, requires neither YidC nor PMF for membrane insertion, while its mutant, V15D, with increased N-terminal negative charges requires both YidC and PMF (Zhu et al, 2013).…”

Section: Interaction Between Membrane Protein Integrase and Yidcmentioning

confidence: 99%

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Interaction between glycolipid MPIase and proteinaceous factors during protein integration into the cytoplasmic membrane of E. coli

Nishikawa

Sawasato

Mori

et al. 2022

Front. Mol. Biosci.

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Protein integration into biomembranes is an essential biological phenomenon common to all organisms. While various factors involved in protein integration, such as SRP, SecYEG and YidC, are proteinaceous, we identified a glycolipid named MPIase (Membrane Protein Integrase), which is present in the cytoplasmic membrane of E. coli. In vitro experiments using inverted membrane vesicles prepared from MPIase-depleted strains, and liposomes containing MPIase showed that MPIase is required for insertion of a subset of membrane proteins, which has been thought to be SecYEG-independent and YidC-dependent. Also, SecYEG-dependent substrate membrane proteins require MPIase in addition. Furthermore, MPIase is also essential for insertion of proteins with multiple negative charges, which requires both YidC and the proton motive force (PMF). MPIase directly interacts with SecYEG and YidC on the membrane. MPIase not only cooperates with these factors but also has a molecular chaperone-like function specific to the substrate membrane proteins through direct interaction with the glycan chain. Thus, MPIase catalyzes membrane insertion by accepting nascent membrane proteins on the membrane through its chaperone-like function, i.e., direct interaction with the substrate proteins, and then MPIase functionally interacts with SecYEG and YidC for substrate delivery, and acts with PMF to facilitate and complete membrane insertion when necessary. In this review, we will outline the mechanisms underlying membrane insertion catalyzed by MPIase, which cooperates with proteinaceous factors and PMF.

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Section: Interaction Between Membrane Protein Integrase and Yidcmentioning

confidence: 80%

Section: Interaction Between Membrane Protein Integrase and Yidcmentioning

confidence: 99%

Interaction between glycolipid MPIase and proteinaceous factors during protein integration into the cytoplasmic membrane of E. coli

Nishikawa

Sawasato

Mori

et al. 2022

Front. Mol. Biosci.

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“…Our recent study revealed that the protein released from the ribosome is captured by sugar chains of MPIase and attracted to the membrane surface through the pyrophosphate group 18 . In the presence of MPIase, some hydrophobic proteins such as the 3L-Pf3 coat, a mutant version of bacteriophage Pf3 coat protein, are inserted into the membrane without YidC, while YidC accelerates the insertion in combination with MPIase 19 , 20 . Therefore, we speculated that the hydrophobic region of the protein would be inserted into the membrane and the hydrophilic region would be delivered into YidC after attraction by MPIase.…”

Section: Introductionmentioning

confidence: 99%

Role of a bacterial glycolipid in Sec-independent membrane protein insertion

Nomura

Mori

Fujikawa

et al. 2022

Sci Rep

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Non-proteinaceous components in membranes regulate membrane protein insertion cooperatively with proteinaceous translocons. An endogenous glycolipid in the Escherichia coli membrane called membrane protein integrase (MPIase) is one such component. Here, we focused on the Sec translocon-independent pathway and examined the mechanisms of MPIase-facilitated protein insertion using physicochemical techniques. We determined the membrane insertion efficiency of a small hydrophobic protein using solid-state nuclear magnetic resonance, which showed good agreement with that determined by the insertion assay using an in vitro translation system. The observed insertion efficiency was strongly correlated with membrane physicochemical properties measured using fluorescence techniques. Diacylglycerol, a trace component of E. coli membrane, reduced the acyl chain mobility in the core region and inhibited the insertion, whereas MPIase restored them. We observed the electrostatic intermolecular interactions between MPIase and the side chain of basic amino acids in the protein, suggesting that the negatively charged pyrophosphate of MPIase attracts the positively charged residues of a protein near the membrane surface, which triggers the insertion. Thus, this study demonstrated the ingenious approach of MPIase to support membrane insertion of proteins by using its unique molecular structure in various ways.

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“…However, many studies have demonstrated that YidC is fundamental for the addition of small phage coat proteins like Pf3 coat and M13 in a Sec-free pathway. 9,[26][27][28][29][30][31] A few experimental studies have explored the role of YidC in various microbial creatures. The genomes of most gram-positive microscopic organisms encode two YidC proteins:…”

Section: Introductionmentioning

confidence: 99%

“…However, many studies have demonstrated that YidC is fundamental for the addition of small phage coat proteins like Pf3 coat and M13 in a Sec-free pathway. 9,26–31…”

Section: Introductionmentioning

confidence: 99%

An Investigation of the YidC-Mediated Membrane Insertion of Pf3 Coat Protein Using Molecular Dynamics Simulations

Polasa

Hettige

Immadisetty

et al. 2022

Preprint

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YidC is a membrane protein that facilitates the insertion of newly synthesized proteins into lipid membranes. Through YidC, proteins are inserted into the lipid bilayer via the SecYEG-dependent complex. Additionally, YidC functions as a chaperone in protein folding processes. Several studies have provided evidence of its independent insertion mechanism. However, the mechanistic details of the YidC independent protein insertion mechanism remain elusive at the molecular level. This study elucidates the insertion mechanism of YidC at an atomic level through a combination of equilibrium and non-equilibrium molecular dynamics (MD) simulations. Different docking models of YidC-Pf3 in the lipid bilayer were built in this study to better understand the insertion mechanism. To conduct a complete investigation of the conformational difference between the two docking models developed, we used classical molecular dynamics simulations supplemented with a non-equilibrium technique. Our findings indicate that the YidC transmembrane (TM) groove is essential for this high-affinity interaction and that the hydrophilic nature of the YidC groove plays an important role in protein transport across the cytoplasmic membrane bilayer to the periplasmic side. At different stages of the insertion process, conformational changes in YidC’s TM domain and membrane core have a mechanistic effect on the Pf3 coat. Furthermore, during the insertion phase, the hydration and dehydration of the YidC’s hydrophilic groove are critical. These demonstrate that Pf3 interactions with the membrane and YidC vary in different conformational states during the insertion process. Finally, this extensive study directly confirms that YidC functions as an independent insertase.

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Interplay between MPIase, YidC, and PMF during Sec-independent insertion of membrane proteins

Cited by 20 publications

References 34 publications

Interaction between glycolipid MPIase and proteinaceous factors during protein integration into the cytoplasmic membrane of E. coli

Interaction between glycolipid MPIase and proteinaceous factors during protein integration into the cytoplasmic membrane of E. coli

Role of a bacterial glycolipid in Sec-independent membrane protein insertion

An Investigation of the YidC-Mediated Membrane Insertion of Pf3 Coat Protein Using Molecular Dynamics Simulations

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