Matches in SemOpenAlex for { <https://semopenalex.org/work/W2766888512> ?p ?o ?g. }
- W2766888512 endingPage "20743" @default.
- W2766888512 startingPage "20732" @default.
- W2766888512 abstract "The bacterial cell division regulators MinD and MinE together with the division inhibitor MinC localize to the membrane in concentrated zones undergoing coordinated pole-to-pole oscillation to help ensure that the cytokinetic division septum forms only at the mid-cell position. This dynamic localization is driven by MinD-catalyzed ATP hydrolysis, stimulated by interactions with MinE’s anti-MinCD domain. This domain is buried in the 6-β–stranded MinE “closed” structure, but is liberated for interactions with MinD, giving rise to a 4-β–stranded “open” structure through an unknown mechanism. Here we show that MinE–membrane interactions induce a structural change into a state resembling the open conformation. However, MinE mutants lacking the MinE membrane-targeting sequence stimulated higher ATP hydrolysis rates than the full-length protein, indicating that binding to MinD is sufficient to trigger this conformational transition in MinE. In contrast, conformational change between the open and closed states did not affect stimulation of ATP hydrolysis rates in the absence of membrane binding, although the MinD-binding residue Ile-25 is critical for this conformational transition. We therefore propose an updated model where MinE is brought to the membrane through interactions with MinD. After stimulation of ATP hydrolysis, MinE remains bound to the membrane in a state that does not catalyze additional rounds of ATP hydrolysis. Although the molecular basis for this inhibited state is unknown, previous observations of higher-order MinE self-association may explain this inhibition. Overall, our findings have general implications for Min protein oscillation cycles, including those that regulate cell division in bacterial pathogens. The bacterial cell division regulators MinD and MinE together with the division inhibitor MinC localize to the membrane in concentrated zones undergoing coordinated pole-to-pole oscillation to help ensure that the cytokinetic division septum forms only at the mid-cell position. This dynamic localization is driven by MinD-catalyzed ATP hydrolysis, stimulated by interactions with MinE’s anti-MinCD domain. This domain is buried in the 6-β–stranded MinE “closed” structure, but is liberated for interactions with MinD, giving rise to a 4-β–stranded “open” structure through an unknown mechanism. Here we show that MinE–membrane interactions induce a structural change into a state resembling the open conformation. However, MinE mutants lacking the MinE membrane-targeting sequence stimulated higher ATP hydrolysis rates than the full-length protein, indicating that binding to MinD is sufficient to trigger this conformational transition in MinE. In contrast, conformational change between the open and closed states did not affect stimulation of ATP hydrolysis rates in the absence of membrane binding, although the MinD-binding residue Ile-25 is critical for this conformational transition. We therefore propose an updated model where MinE is brought to the membrane through interactions with MinD. After stimulation of ATP hydrolysis, MinE remains bound to the membrane in a state that does not catalyze additional rounds of ATP hydrolysis. Although the molecular basis for this inhibited state is unknown, previous observations of higher-order MinE self-association may explain this inhibition. Overall, our findings have general implications for Min protein oscillation cycles, including those that regulate cell division in bacterial pathogens." @default.
- W2766888512 created "2017-11-10" @default.
- W2766888512 creator A5009262851 @default.
- W2766888512 creator A5013565841 @default.
- W2766888512 creator A5021761565 @default.
- W2766888512 creator A5047556356 @default.
- W2766888512 creator A5073712525 @default.
- W2766888512 creator A5081540235 @default.
- W2766888512 date "2017-12-01" @default.
- W2766888512 modified "2023-10-06" @default.
- W2766888512 title "Dissecting the role of conformational change and membrane binding by the bacterial cell division regulator MinE in the stimulation of MinD ATPase activity" @default.
- W2766888512 cites W1485168135 @default.
- W2766888512 cites W1527686785 @default.
- W2766888512 cites W1549355483 @default.
- W2766888512 cites W1570192829 @default.
- W2766888512 cites W1597706240 @default.
- W2766888512 cites W1778557300 @default.
- W2766888512 cites W1846301815 @default.
- W2766888512 cites W1879208270 @default.
- W2766888512 cites W1895202121 @default.
- W2766888512 cites W1919469224 @default.
- W2766888512 cites W1943903427 @default.
- W2766888512 cites W1963762739 @default.
- W2766888512 cites W1967593111 @default.
- W2766888512 cites W1977050371 @default.
- W2766888512 cites W1978195377 @default.
- W2766888512 cites W1980532227 @default.
- W2766888512 cites W1989270637 @default.
- W2766888512 cites W2000711487 @default.
- W2766888512 cites W2003561881 @default.
- W2766888512 cites W2008228685 @default.
- W2766888512 cites W2008433064 @default.
- W2766888512 cites W2008817593 @default.
- W2766888512 cites W2009415450 @default.
- W2766888512 cites W2010195422 @default.
- W2766888512 cites W2014495166 @default.
- W2766888512 cites W2018291538 @default.
- W2766888512 cites W2020294018 @default.
- W2766888512 cites W2029807656 @default.
- W2766888512 cites W2033350939 @default.
- W2766888512 cites W2039870129 @default.
- W2766888512 cites W2045579841 @default.
- W2766888512 cites W2056816046 @default.
- W2766888512 cites W2057251045 @default.
- W2766888512 cites W2062336984 @default.
- W2766888512 cites W2072890077 @default.
- W2766888512 cites W2077176951 @default.
- W2766888512 cites W2081395979 @default.
- W2766888512 cites W2081553155 @default.
- W2766888512 cites W2082176639 @default.
- W2766888512 cites W2088848851 @default.
- W2766888512 cites W2088852581 @default.
- W2766888512 cites W2090866085 @default.
- W2766888512 cites W2093727932 @default.
- W2766888512 cites W2099904987 @default.
- W2766888512 cites W2100280493 @default.
- W2766888512 cites W2105322190 @default.
- W2766888512 cites W2106464635 @default.
- W2766888512 cites W2117750363 @default.
- W2766888512 cites W2127811731 @default.
- W2766888512 cites W2131252553 @default.
- W2766888512 cites W2132180320 @default.
- W2766888512 cites W2135336327 @default.
- W2766888512 cites W2137015675 @default.
- W2766888512 cites W2142104231 @default.
- W2766888512 cites W2147715031 @default.
- W2766888512 cites W2148571760 @default.
- W2766888512 cites W2153979160 @default.
- W2766888512 cites W2156977920 @default.
- W2766888512 cites W2162085395 @default.
- W2766888512 cites W2163479977 @default.
- W2766888512 cites W2167490524 @default.
- W2766888512 cites W2169821755 @default.
- W2766888512 cites W2287972295 @default.
- W2766888512 cites W2657598059 @default.
- W2766888512 cites W2950192057 @default.
- W2766888512 cites W2983308323 @default.
- W2766888512 cites W3124033058 @default.
- W2766888512 cites W396269583 @default.
- W2766888512 cites W2145800641 @default.
- W2766888512 doi "https://doi.org/10.1074/jbc.m117.805945" @default.
- W2766888512 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5733608" @default.
- W2766888512 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29066619" @default.
- W2766888512 hasPublicationYear "2017" @default.
- W2766888512 type Work @default.
- W2766888512 sameAs 2766888512 @default.
- W2766888512 citedByCount "16" @default.
- W2766888512 countsByYear W27668885122018 @default.
- W2766888512 countsByYear W27668885122019 @default.
- W2766888512 countsByYear W27668885122020 @default.
- W2766888512 countsByYear W27668885122021 @default.
- W2766888512 countsByYear W27668885122023 @default.
- W2766888512 crossrefType "journal-article" @default.
- W2766888512 hasAuthorship W2766888512A5009262851 @default.
- W2766888512 hasAuthorship W2766888512A5013565841 @default.
- W2766888512 hasAuthorship W2766888512A5021761565 @default.
- W2766888512 hasAuthorship W2766888512A5047556356 @default.
- W2766888512 hasAuthorship W2766888512A5073712525 @default.