A multienzyme complex channels substrates and electrons through acetyl-CoA and methane biosynthesis pathways in Methanosarcina.
Multienzyme complexes catalyze important metabolic reactions in many organisms, but little is known about the complexes involved in biological methane production (methanogenesis). A crosslinking-mass spectrometry (XL-MS) strategy was employed to identify proteins associated with coenzyme M-coenzyme...
Guardado en:
| Autores principales: | , , , , , , |
|---|---|
| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Public Library of Science (PLoS)
2014
|
| Materias: | |
| Acceso en línea: | https://doaj.org/article/267118d4672a437c84db44e6dc356484 |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| id |
oai:doaj.org-article:267118d4672a437c84db44e6dc356484 |
|---|---|
| record_format |
dspace |
| spelling |
oai:doaj.org-article:267118d4672a437c84db44e6dc3564842021-11-25T06:00:14ZA multienzyme complex channels substrates and electrons through acetyl-CoA and methane biosynthesis pathways in Methanosarcina.1932-620310.1371/journal.pone.0107563https://doaj.org/article/267118d4672a437c84db44e6dc3564842014-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0107563https://doaj.org/toc/1932-6203Multienzyme complexes catalyze important metabolic reactions in many organisms, but little is known about the complexes involved in biological methane production (methanogenesis). A crosslinking-mass spectrometry (XL-MS) strategy was employed to identify proteins associated with coenzyme M-coenzyme B heterodisulfide reductase (Hdr), an essential enzyme in all methane-producing archaea (methanogens). In Methanosarcina acetivorans, Hdr forms a multienzyme complex with acetyl-CoA decarbonylase synthase (ACDS), and F420-dependent methylene-H4MPT reductase (Mer). ACDS is essential for production of acetyl-CoA during growth on methanol, or for methanogenesis from acetate, whereas Mer is essential for methanogenesis from all substrates. Existence of a Hdr:ACDS:Mer complex is consistent with growth phenotypes of ACDS and Mer mutant strains in which the complex samples the redox status of electron carriers and directs carbon flux to acetyl-CoA or methanogenesis. We propose the Hdr:ACDS:Mer complex comprises a special class of multienzyme redox complex which functions as a "biological router" that physically links methanogenesis and acetyl-CoA biosynthesis pathways.Dillon J LieberJennifer CatlettNandu MadayiputhiyaRenu NandakumarMadeline M LopezWilliam W MetcalfNicole R BuanPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 9, p e107563 (2014) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Medicine R Science Q |
| spellingShingle |
Medicine R Science Q Dillon J Lieber Jennifer Catlett Nandu Madayiputhiya Renu Nandakumar Madeline M Lopez William W Metcalf Nicole R Buan A multienzyme complex channels substrates and electrons through acetyl-CoA and methane biosynthesis pathways in Methanosarcina. |
| description |
Multienzyme complexes catalyze important metabolic reactions in many organisms, but little is known about the complexes involved in biological methane production (methanogenesis). A crosslinking-mass spectrometry (XL-MS) strategy was employed to identify proteins associated with coenzyme M-coenzyme B heterodisulfide reductase (Hdr), an essential enzyme in all methane-producing archaea (methanogens). In Methanosarcina acetivorans, Hdr forms a multienzyme complex with acetyl-CoA decarbonylase synthase (ACDS), and F420-dependent methylene-H4MPT reductase (Mer). ACDS is essential for production of acetyl-CoA during growth on methanol, or for methanogenesis from acetate, whereas Mer is essential for methanogenesis from all substrates. Existence of a Hdr:ACDS:Mer complex is consistent with growth phenotypes of ACDS and Mer mutant strains in which the complex samples the redox status of electron carriers and directs carbon flux to acetyl-CoA or methanogenesis. We propose the Hdr:ACDS:Mer complex comprises a special class of multienzyme redox complex which functions as a "biological router" that physically links methanogenesis and acetyl-CoA biosynthesis pathways. |
| format |
article |
| author |
Dillon J Lieber Jennifer Catlett Nandu Madayiputhiya Renu Nandakumar Madeline M Lopez William W Metcalf Nicole R Buan |
| author_facet |
Dillon J Lieber Jennifer Catlett Nandu Madayiputhiya Renu Nandakumar Madeline M Lopez William W Metcalf Nicole R Buan |
| author_sort |
Dillon J Lieber |
| title |
A multienzyme complex channels substrates and electrons through acetyl-CoA and methane biosynthesis pathways in Methanosarcina. |
| title_short |
A multienzyme complex channels substrates and electrons through acetyl-CoA and methane biosynthesis pathways in Methanosarcina. |
| title_full |
A multienzyme complex channels substrates and electrons through acetyl-CoA and methane biosynthesis pathways in Methanosarcina. |
| title_fullStr |
A multienzyme complex channels substrates and electrons through acetyl-CoA and methane biosynthesis pathways in Methanosarcina. |
| title_full_unstemmed |
A multienzyme complex channels substrates and electrons through acetyl-CoA and methane biosynthesis pathways in Methanosarcina. |
| title_sort |
multienzyme complex channels substrates and electrons through acetyl-coa and methane biosynthesis pathways in methanosarcina. |
| publisher |
Public Library of Science (PLoS) |
| publishDate |
2014 |
| url |
https://doaj.org/article/267118d4672a437c84db44e6dc356484 |
| work_keys_str_mv |
AT dillonjlieber amultienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT jennifercatlett amultienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT nandumadayiputhiya amultienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT renunandakumar amultienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT madelinemlopez amultienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT williamwmetcalf amultienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT nicolerbuan amultienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT dillonjlieber multienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT jennifercatlett multienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT nandumadayiputhiya multienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT renunandakumar multienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT madelinemlopez multienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT williamwmetcalf multienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina AT nicolerbuan multienzymecomplexchannelssubstratesandelectronsthroughacetylcoaandmethanebiosynthesispathwaysinmethanosarcina |
| _version_ |
1718414269949673472 |