Probabilistic Study on Subunit Mismatch Arrangement in Staphylococcal γ-hemolysin Heteroheptameric Transmembrane Pore
Staphylococcal γ-hemolysin (Hlg), consists of two separate proteins, Hlg1 (LukF) of 34 kDa and Hlg2 of 32 kDa, which cooperatively lyse mammalian erythrocytes. Hlg is an illustrative molecule for the study of the assembly and membrane insertion of transmembrane proteins having the unique c...
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| Format: | Article |
| Language: | English |
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The Japan Society of Mechanical Engineers
2011-10-01
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| Series: | Journal of Biomechanical Science and Engineering |
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| Online Access: | https://www.jstage.jst.go.jp/article/jbse/6/4/6_4_286/_pdf/-char/en |
| _version_ | 1828782175989792768 |
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| author | Noriko TOMITA Kazuyo ABE Jun KANEKO Yoshiyuki KAMIO Makoto OHTA |
| author_facet | Noriko TOMITA Kazuyo ABE Jun KANEKO Yoshiyuki KAMIO Makoto OHTA |
| author_sort | Noriko TOMITA |
| collection | DOAJ |
| description | Staphylococcal γ-hemolysin (Hlg), consists of two separate proteins, Hlg1 (LukF) of 34 kDa and Hlg2 of 32 kDa, which cooperatively lyse mammalian erythrocytes. Hlg is an illustrative molecule for the study of the assembly and membrane insertion of transmembrane proteins having the unique characteristic of being composed of two separate proteins. Our previous studies revealed that LukF and Hlg2 assemble alternately on a membrane to form ring-shaped heteroheptameric transmembrane pores, which form funnel-shaped structure with a subunit mismatch arrangement in which the distance between two of the adjacent subunits is significant larger than the others. In the present study, further analysis of the subunit mismatch arrangement in Hlg heteroheptameric pores was conducted by two-dimensional (2-D) image analysis. The distances between two adjacent subunits were numbered according to the size of the distance between adjacent subunits, and how each distance was arranged in the pore was investigated. As a result, the following results were clarified: (1) Not all distances between two adjacent subunits are even. This indicates that a mismatch arrangement exists at not only one site but also at other sites. (2) There is a high probability leading several patterns of mismatch arrangement. (3) These mismatch patterns tend to be polarized into a region in which the distance between subunits is great and a region in which such distance is small. The probabilistic analysis used in this study revealed that there is the intrinsic geometry with subunit arrangements in the heteroheptameric pore consists of two differential subunits. |
| first_indexed | 2024-12-11T17:45:32Z |
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| id | doaj.art-5cfdf4229d5c44a892d62f28a2c95847 |
| institution | Directory Open Access Journal |
| issn | 1880-9863 |
| language | English |
| last_indexed | 2024-12-11T17:45:32Z |
| publishDate | 2011-10-01 |
| publisher | The Japan Society of Mechanical Engineers |
| record_format | Article |
| series | Journal of Biomechanical Science and Engineering |
| spelling | doaj.art-5cfdf4229d5c44a892d62f28a2c958472022-12-22T00:56:24ZengThe Japan Society of Mechanical EngineersJournal of Biomechanical Science and Engineering1880-98632011-10-016428629810.1299/jbse.6.286jbseProbabilistic Study on Subunit Mismatch Arrangement in Staphylococcal γ-hemolysin Heteroheptameric Transmembrane PoreNoriko TOMITA0Kazuyo ABE1Jun KANEKO2Yoshiyuki KAMIO3Makoto OHTA4Institute of Fluid science, Tohoku UniversityInstitute of Fluid science, Tohoku UniversityDepartment of Microbial Biotechnology, Graduate School of Agricultural Science, Tohoku UniversityDepartment of Biomechanical Engineering, Graduate School of Science and Engineering, Yamagata UniversityInstitute of Fluid science, Tohoku UniversityStaphylococcal γ-hemolysin (Hlg), consists of two separate proteins, Hlg1 (LukF) of 34 kDa and Hlg2 of 32 kDa, which cooperatively lyse mammalian erythrocytes. Hlg is an illustrative molecule for the study of the assembly and membrane insertion of transmembrane proteins having the unique characteristic of being composed of two separate proteins. Our previous studies revealed that LukF and Hlg2 assemble alternately on a membrane to form ring-shaped heteroheptameric transmembrane pores, which form funnel-shaped structure with a subunit mismatch arrangement in which the distance between two of the adjacent subunits is significant larger than the others. In the present study, further analysis of the subunit mismatch arrangement in Hlg heteroheptameric pores was conducted by two-dimensional (2-D) image analysis. The distances between two adjacent subunits were numbered according to the size of the distance between adjacent subunits, and how each distance was arranged in the pore was investigated. As a result, the following results were clarified: (1) Not all distances between two adjacent subunits are even. This indicates that a mismatch arrangement exists at not only one site but also at other sites. (2) There is a high probability leading several patterns of mismatch arrangement. (3) These mismatch patterns tend to be polarized into a region in which the distance between subunits is great and a region in which such distance is small. The probabilistic analysis used in this study revealed that there is the intrinsic geometry with subunit arrangements in the heteroheptameric pore consists of two differential subunits.https://www.jstage.jst.go.jp/article/jbse/6/4/6_4_286/_pdf/-char/enstaphylococcal γ-hemolysintwo-component hemolysinpore-forming toxinheteroheptamertransmission electron microscopyprobabilistic analysissubunit mismatch arrangement |
| spellingShingle | Noriko TOMITA Kazuyo ABE Jun KANEKO Yoshiyuki KAMIO Makoto OHTA Probabilistic Study on Subunit Mismatch Arrangement in Staphylococcal γ-hemolysin Heteroheptameric Transmembrane Pore Journal of Biomechanical Science and Engineering staphylococcal γ-hemolysin two-component hemolysin pore-forming toxin heteroheptamer transmission electron microscopy probabilistic analysis subunit mismatch arrangement |
| title | Probabilistic Study on Subunit Mismatch Arrangement in Staphylococcal γ-hemolysin Heteroheptameric Transmembrane Pore |
| title_full | Probabilistic Study on Subunit Mismatch Arrangement in Staphylococcal γ-hemolysin Heteroheptameric Transmembrane Pore |
| title_fullStr | Probabilistic Study on Subunit Mismatch Arrangement in Staphylococcal γ-hemolysin Heteroheptameric Transmembrane Pore |
| title_full_unstemmed | Probabilistic Study on Subunit Mismatch Arrangement in Staphylococcal γ-hemolysin Heteroheptameric Transmembrane Pore |
| title_short | Probabilistic Study on Subunit Mismatch Arrangement in Staphylococcal γ-hemolysin Heteroheptameric Transmembrane Pore |
| title_sort | probabilistic study on subunit mismatch arrangement in staphylococcal gamma hemolysin heteroheptameric transmembrane pore |
| topic | staphylococcal γ-hemolysin two-component hemolysin pore-forming toxin heteroheptamer transmission electron microscopy probabilistic analysis subunit mismatch arrangement |
| url | https://www.jstage.jst.go.jp/article/jbse/6/4/6_4_286/_pdf/-char/en |
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