<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7(6)</volume><submitter>Che L</submitter><pubmed_abstract>Cyanobacterial NdhM, an oxygenic photosynthesis-specific NDH-1 subunit, has been found to be essential for the formation of a large complex of NDH-1 (NDH-1L). The cryo-electron microscopic (cryo-EM) structure of NdhM from &lt;i>Thermosynechococcus elongatus&lt;/i> showed that the N-terminus of NdhM contains three β-sheets, while two α-helixes are present in the middle and C-terminal part of NdhM. Here, we obtained a mutant of the unicellular cyanobacterium &lt;i>Synechocystis&lt;/i> 6803 expressing a C-terminal truncated NdhM subunit designated NdhMΔC. Accumulation and activity of NDH-1 were not affected in NdhMΔC under normal growth conditions. However, the NDH-1 complex with truncated NdhM is unstable under stress. Immunoblot analyses showed that the assembly process of the cyanobacterial NDH-1L hyd</pubmed_abstract><journal>Plant direct</journal><pagination>e502</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10272980</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>NDH-1L with a truncated NdhM subunit is unstable under stress conditions in cyanobacteria.</pubmed_title><pmcid>PMC10272980</pmcid><pubmed_authors>Huang Y</pubmed_authors><pubmed_authors>Guo Y</pubmed_authors><pubmed_authors>Che L</pubmed_authors><pubmed_authors>Peng L</pubmed_authors><pubmed_authors>Gao F</pubmed_authors></additional><is_claimable>false</is_claimable><name>NDH-1L with a truncated NdhM subunit is unstable under stress conditions in cyanobacteria.</name><description>Cyanobacterial NdhM, an oxygenic photosynthesis-specific NDH-1 subunit, has been found to be essential for the formation of a large complex of NDH-1 (NDH-1L). The cryo-electron microscopic (cryo-EM) structure of NdhM from &lt;i>Thermosynechococcus elongatus&lt;/i> showed that the N-terminus of NdhM contains three β-sheets, while two α-helixes are present in the middle and C-terminal part of NdhM. Here, we obtained a mutant of the unicellular cyanobacterium &lt;i>Synechocystis&lt;/i> 6803 expressing a C-terminal truncated NdhM subunit designated NdhMΔC. Accumulation and activity of NDH-1 were not affected in NdhMΔC under normal growth conditions. However, the NDH-1 complex with truncated NdhM is unstable under stress. Immunoblot analyses showed that the assembly process of the cyanobacterial NDH-1L hyd</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Jun</publication><modification>2026-04-29T02:28:31.178Z</modification><creation>2025-02-19T04:01:43.24Z</creation></dates><accession>S-EPMC10272980</accession><cross_references><pubmed>37334271</pubmed><doi>10.1002/pld3.502</doi></cross_references></HashMap>