Bacterial tail anchors can target to the mitochondrial outer membrane

Lutfullahoğlu-Bal, Güleycan; Keskin, Abdurrahman; Seferoglu, Ayse Bengisu; Dunn, Cory D.

doi:10.1186/s13062-017-0187-0

Cited by 13 publications

(16 citation statements)

References 56 publications

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“…In this study, we have demonstrated that a predicted membrane insertion sequence obtained from a prokaryote can be directed to the peroxisomes of eukaryotic cells. Our findings expand upon earlier studies in which protein sequence derived from prokaryotes could traffic to eukaryotic organelles, such as ER and mitochondria 25,[61][62][63][64][65] . We propose that the ability to direct prokaryotic protein sequences to eukaryotic organelles, even though these regions were not previously selected for targeting prowess in eukaryotes, might have been of general benefit to eukaryotes over evolutionary time.…”

Section: Why Is Protein Targeting To Eukaryotic Organelles So Permisssupporting

confidence: 84%

“…The E. coli YgiM(TA) was detected at peroxisomes, with no microscopic or functional evidence of mitochondrial localization in yeast or in human cells. Conversely, TAs found within two other proteins encoded by the same organism, YqjD and ElaB, targeted to mitochondria and ER, with no evidence of peroxisomal localization 25 [and this study]. Other tail-anchored proteins can target to both mitochondria and peroxisomes.…”

Section: What Features Of Ygim(ta) Allow Targeting To Peroxisomes?mentioning

confidence: 68%

“…2c and 2e). Not all bacteria-derived TAs can support Pex15p function: Pex15(1-331) fused to the E. coli YqjD(TA), which was previously demonstrated 25 to target predominantly to mitochondria and, to a lesser extent, the ER, failed to allow pex15∆ rescue ( Fig. 2d and 2e).…”

Section: The Ygim Tail Anchor Can Functionally Replace An Endogenousmentioning

confidence: 96%

“…During a previous appraisal of the ability of eukaryotic cells to utilize potential targeting information encoded by prokaryotes 25 , we fused mCherry to the amino-terminus of TAs predicted to be encoded by the E. coli genome. These fluorescent fusion proteins were found at diverse locations within the cell, and we noted that mCherry fused to amino acids 173-206 of the uncharacterized YgiM protein, hereafter called the YgiM(TA), was found in a punctate pattern reminiscent of peroxisomes.…”

Section: A Domain Encoded By the Bacterial Ygim Protein Is Targeted Tmentioning

confidence: 99%

“…Signals found within the polypeptide sequence of nucleus-encoded genes play a dominant role in targeting to eukaryotic organelles, and how prokaryote-derived proteins might acquire such sequences and become localized to eukaryotic organelles is a topic of intense inquiry. In a previous study 25 directed toward the principals of organelle targeting following HGT from bacteria, we focused our attention upon those proteins predicted to be anchored to membranes by a carboxyl-terminal hydrophobic stretch of amino acids, or a tail anchor (TA). Here, we describe the trafficking of one of these bacteria-derived TAs, retrieved from the YgiM protein of E. coli.…”

Section: Introductionmentioning

confidence: 99%

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A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells

Lutfullahoğlu-Bal

Seferoglu

Keskin

et al. 2018

Preprint

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This is a version of the manuscript prepared prior to incorporation of peer-reviewer comments. 2 ABSTRACTProkaryotes can provide new genetic information to eukaryotes by horizontal gene transfer (HGT), and such transfers are likely to have been particularly consequential at the dawn of eukaryogenesis. Since eukaryotes are highly compartmentalized, it is worthwhile to consider the mechanisms by which newly transferred proteins might reach diverse organellar destinations. Toward this goal, we have focused our attention upon the behavior of bacteria-derived tail anchors (TAs) expressed in the eukaryote Saccharomyces cerevisiae. In this study, we report that a predicted membrane-associated domain of the Escherichia coli YgiM protein is specifically trafficked to peroxisomes in budding yeast, can be found at a pre-peroxisomal compartment (PPC) upon disruption of peroxisomal biogenesis, and can functionally replace an endogenous peroxisome-directed TA. Furthermore, the YgiM(TA) can also localize to peroxisomes in mammalian cells. Since the YgiM(TA) plays no endogenous role in peroxisomal function or assembly, this domain is likely to serve as an excellent tool toward illumination of the mechanisms by which TAs can travel to peroxisomes. Moreover, our findings emphasize the ease with which bacteria-derived sequences might target to organelles in eukaryotic cells following HGT, and we discuss the importance of flexible recognition of organelle targeting information during and after eukaryogenesis.

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Section: Why Is Protein Targeting To Eukaryotic Organelles So Permisssupporting

confidence: 84%

Section: What Features Of Ygim(ta) Allow Targeting To Peroxisomes?mentioning

confidence: 68%

Section: The Ygim Tail Anchor Can Functionally Replace An Endogenousmentioning

confidence: 96%

Section: A Domain Encoded By the Bacterial Ygim Protein Is Targeted Tmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells

Lutfullahoğlu-Bal

Seferoglu

Keskin

et al. 2018

Preprint

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Evolutionarily conserved mechanism for membrane recognition from bacteria to mitochondria

2021

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The mechanisms controlling membrane recognition by proteins with one hydrophobic stretch at their carboxyl terminus (tail anchor, TA) are poorly defined. The Escherichia coli TAs of ElaB and YqjD, which share sequential and structural similarity with the Saccharomyces cerevisiae TA of Fis1, were shown to localize to mitochondria. We show that YqjD and ElaB are directed by their TAs to bacterial cell poles. Fis1(TA) expressed in E. coli localizes like the endogenous TAs. The yeast and bacterial TAs are inserted in the E. coli inner membrane, and they all show affiliation to phosphatidic acid (PA), found in the membrane of the bacterial cell poles and of the yeast mitochondria. Our results suggest a mechanism for TA membrane recognition conserved from bacteria to mitochondria and raise the possibility that through their interaction with PA, and TAs play a role across prokaryotes and eukaryotes in controlling cell/organelle fate.

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The MICOS Complex Subunit Mic60 is Hijacked by Intracellular Bacteria to Manipulate Mitochondrial Dynamics and Promote Bacterial Pathogenicity

Cheng,

Chen,

Sun

et al. 2024

Advanced Science

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Host mitochondria undergo fission and fusion, which bacteria often exploit for their infections. In this study, the underlying molecular mechanisms are aimed to clarify through which Listeria monocytogenes (L. monocytogenes), a human bacterial pathogen, manipulates mitochondrial dynamics to enhance its pathogenicity. It is demonstrated that L. monocytogenes triggers transient mitochondrial fission through its virulence factor listeriolysin O (LLO), driven by LLO's interaction with Mic60, a core component of the mitochondrial contact site and the cristae organizing system (MICOS). Specifically, Phe251 within LLO is identify as a crucial residue for binding to Mic60, crucial for LLO‐induced mitochondrial fragmentation and bacterial pathogenicity. Importantly, it is that Mic60 affect the formation of F‐actin tails recruited by L. monocytogenes, thereby contributing to intracellular bacterial infection. Mic60 plays a critical role in mediating changes in mitochondrial morphology, membrane potential, and reactive oxidative species (ROS) production, and L. monocytogenes infection exacerbates these changes by affecting Mic60 expression. These findings unveil a novel mechanism through which intracellular bacteria exploit host mitochondria, shedding light on the complex interplay between hosts and microbes during infections. This knowledge holds promise for developing innovative strategies to combat bacterial infections.

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Bacterial tail anchors can target to the mitochondrial outer membrane

Cited by 13 publications

References 56 publications

A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells

A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells

Evolutionarily conserved mechanism for membrane recognition from bacteria to mitochondria

The MICOS Complex Subunit Mic60 is Hijacked by Intracellular Bacteria to Manipulate Mitochondrial Dynamics and Promote Bacterial Pathogenicity

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