Details
| Translated title of the contribution | Vorkommen und potentieller Mechanismus des Holin-vermittelten nicht-lytischen Proteintransports in Bakterien |
|---|---|
| Original language | English |
| Pages (from-to) | 159 - 173 |
| Number of pages | 15 |
| Journal | Microbial Cell |
| Volume | 9 |
| Issue number | 10 |
| Publication status | Published - 23 Sept 2022 |
Abstract
Holins are generally believed to generate large membrane lesions that permit the passage of endolysins across the cytoplasmic membrane of prokaryotes, ultimately resulting in cell wall degradation and cell lysis. However, there are more and more examples known for non-lytic holin-dependent secretion of proteins by bacteria, indicating that holins somehow can transport proteins without causing large membrane lesions. Phage-derived holins can be used for a non-lytic endolysin translocation to permeabilize the cell wall for the passage of secreted proteins. In addition, clostridia, which do not possess the Tat pathway for transport of folded proteins, most likely employ non-lytic holin-mediated transport also for secretion of toxins and bacteriocins that are incompatible with the general Sec pathway. The mechanism for non-lytic holin-mediated transport is unknown, but the recent finding that the small holin TpeE mediates a non-lytic toxin secretion in Clostridium perfringens opened new perspectives. TpeE contains only one short transmembrane helix that is followed by an amphipathic helix, which is reminiscent of TatA, the membrane-permeabilizing component of the Tat translocon for folded proteins. Here we review the known cases of non-lytic holin-mediated transport and then focus on the structural and functional comparison of TatA and TpeE, resulting in a mechanistic model for holin-mediated transport. This model is strongly supported by a so far not recognized naturally occurring holin-endolysin fusion protein.
Keywords
- holins, protein translocation, clostridia, toxins, bacteriocins, endolysins, Tat transport
ASJC Scopus subject areas
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry, Genetics and Molecular Biology (miscellaneous)
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Immunology and Microbiology(all)
- Virology
- Immunology and Microbiology(all)
- Parasitology
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
- Immunology and Microbiology(all)
- Microbiology
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In: Microbial Cell, Vol. 9, No. 10, 23.09.2022, p. 159 - 173.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Occurrence and potential mechanism of holin-mediated non-lytic protein translocation in bacteria
AU - Brüser, Thomas
AU - Mehner-Breitfeld, Denise
N1 - Funding Information: We thank Ralf Gerhard (Medical High School Hannover, Germany) and Jörg Overmann (DSMZ Braunschweig, Germany) for helpful discussions. We thank Anders Krogh (University of Copenhagen, Denmark) for discussion of TMHMM predictions. This study was supported by the state of Lower Saxony.
PY - 2022/9/23
Y1 - 2022/9/23
N2 - Holins are generally believed to generate large membrane lesions that permit the passage of endolysins across the cytoplasmic membrane of prokaryotes, ultimately resulting in cell wall degradation and cell lysis. However, there are more and more examples known for non-lytic holin-dependent secretion of proteins by bacteria, indicating that holins somehow can transport proteins without causing large membrane lesions. Phage-derived holins can be used for a non-lytic endolysin translocation to permeabilize the cell wall for the passage of secreted proteins. In addition, clostridia, which do not possess the Tat pathway for transport of folded proteins, most likely employ non-lytic holin-mediated transport also for secretion of toxins and bacteriocins that are incompatible with the general Sec pathway. The mechanism for non-lytic holin-mediated transport is unknown, but the recent finding that the small holin TpeE mediates a non-lytic toxin secretion in Clostridium perfringens opened new perspectives. TpeE contains only one short transmembrane helix that is followed by an amphipathic helix, which is reminiscent of TatA, the membrane-permeabilizing component of the Tat translocon for folded proteins. Here we review the known cases of non-lytic holin-mediated transport and then focus on the structural and functional comparison of TatA and TpeE, resulting in a mechanistic model for holin-mediated transport. This model is strongly supported by a so far not recognized naturally occurring holin-endolysin fusion protein.
AB - Holins are generally believed to generate large membrane lesions that permit the passage of endolysins across the cytoplasmic membrane of prokaryotes, ultimately resulting in cell wall degradation and cell lysis. However, there are more and more examples known for non-lytic holin-dependent secretion of proteins by bacteria, indicating that holins somehow can transport proteins without causing large membrane lesions. Phage-derived holins can be used for a non-lytic endolysin translocation to permeabilize the cell wall for the passage of secreted proteins. In addition, clostridia, which do not possess the Tat pathway for transport of folded proteins, most likely employ non-lytic holin-mediated transport also for secretion of toxins and bacteriocins that are incompatible with the general Sec pathway. The mechanism for non-lytic holin-mediated transport is unknown, but the recent finding that the small holin TpeE mediates a non-lytic toxin secretion in Clostridium perfringens opened new perspectives. TpeE contains only one short transmembrane helix that is followed by an amphipathic helix, which is reminiscent of TatA, the membrane-permeabilizing component of the Tat translocon for folded proteins. Here we review the known cases of non-lytic holin-mediated transport and then focus on the structural and functional comparison of TatA and TpeE, resulting in a mechanistic model for holin-mediated transport. This model is strongly supported by a so far not recognized naturally occurring holin-endolysin fusion protein.
KW - Holine
KW - Proteintransport
KW - holins
KW - protein translocation
KW - clostridia
KW - toxins
KW - bacteriocins
KW - endolysins
KW - Tat transport
UR - http://www.scopus.com/inward/record.url?scp=85140920595&partnerID=8YFLogxK
U2 - 10.15698/mic2022.10.785
DO - 10.15698/mic2022.10.785
M3 - Article
VL - 9
SP - 159
EP - 173
JO - Microbial Cell
JF - Microbial Cell
IS - 10
ER -