BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism

被引:29
|
作者
Plummer, Ashlee M. [1 ]
Fleming, Karen G. [1 ]
机构
[1] Johns Hopkins Univ, Thomas C Jenkins Dept Biophys, Baltimore, MD 21218 USA
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
ESCHERICHIA-COLI; DODECYL-SULFATE; YAET COMPLEX; BIOGENESIS; CONFORMATION;
D O I
10.1021/acs.biochem.5b00950
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
beta-Barrel assembly machinery protein A (BamA) plays a critical role in the biogenesis of outer membrane proteins (OMPs); however, a mechanistic understanding of its function is lacking. Here, we report an in vitro assay that investigates whether the mechanism of BamA-catalyzed OMP folding is stoichiometric or catalytic. We found that BamA accelerates the folding of OMPs in vitro via a catalytic mechanism, similar to the activity of the full multiprotein beta-barrel assembly machinery (BAM) complex in vivo. As BamA alone can repeatedly facilitate the folding of OMPs, we suggest the additional BAM components accelerate this basal activity to biologically relevant time scales.
引用
收藏
页码:6009 / 6011
页数:3
相关论文
共 50 条
  • [21] Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
    Renault, Marie
    Bos, Martine P.
    Tommassen, Jan
    Baldus, Marc
    JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2011, 133 (12) : 4175 - 4177
  • [22] Lipoprotein DolP supports proper folding of BamA in the bacterial outer membrane promoting fitness upon envelope stress
    Ranava, David
    Yang, Yiying
    Orenday-Tapia, Luis
    Rousset, Francois
    Turlan, Catherine
    Morales, Violette
    Cui, Lun
    Moulin, Cyril
    Froment, Carine
    Munoz, Gladys
    Rech, Jerome
    Marcoux, Julien
    Caumont-Sarcos, Anne
    Albenne, Cecile
    Bikard, David
    Ieva, Raffaele
    ELIFE, 2021, 10
  • [23] Structure and Flexibility of the Complete Periplasmic Domain of BamA: The Protein Insertion Machine of the Outer Membrane
    Gatzeva-Topalova, Petia Zvezdanova
    Warner, Lisa Rosa
    Pardi, Arthur
    Sousa, Marcelo Carlos
    STRUCTURE, 2010, 18 (11) : 1492 - 1501
  • [24] Conformational Plasticity of the POTRA 5 Domain in the Outer Membrane Protein Assembly Factor BamA
    Sinnige, Tessa
    Weingarth, Markus
    Daniels, Mark
    Boelens, Rolf
    Bonvin, Alexandre M. J. J.
    Houben, Klaartje
    Baldus, Marc
    STRUCTURE, 2015, 23 (07) : 1317 - 1324
  • [25] Augmenting β-Augmentation: Structural Basis of How BamB Binds BamA and May Support Folding of Outer Membrane Proteins
    Heuck, Alexander
    Schleiffer, Alexander
    Clausen, Tim
    JOURNAL OF MOLECULAR BIOLOGY, 2011, 406 (05) : 659 - 666
  • [26] The trials and tribulations of membrane protein folding in vitro
    Booth, PJ
    BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2003, 1610 (01): : 51 - 56
  • [27] Folding of a bacterial integral outer membrane protein is initiated in the periplasm
    Rakesh Sikdar
    Janine H. Peterson
    D. Eric Anderson
    Harris D. Bernstein
    Nature Communications, 8
  • [28] Outer membrane protein folding from an energy landscape perspective
    Bob Schiffrin
    David J. Brockwell
    Sheena E. Radford
    BMC Biology, 15
  • [29] Folding of a bacterial integral outer membrane protein is initiated in the periplasm
    Sikdar, Rakesh
    Peterson, Janine H.
    Anderson, D. Eric
    Bernstein, Harris D.
    NATURE COMMUNICATIONS, 2017, 8
  • [30] Outer membrane protein folding from an energy landscape perspective
    Schiffrin, Bob
    Brockwell, David J.
    Radford, Sheena E.
    BMC BIOLOGY, 2017, 15