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

来源：

BIOCHEMISTRY | 2015年 / 54卷 / 39期

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

页码：6009 / 6011

页数：3

共 42 条

[21] Refolding, crystallization and preliminary X-ray crystallographic studies of the β-barrel domain of BamA, a membrane protein essential for outer membrane protein biogenesis [J].

Ni, Dongchun ;

Yang, Kun ;

Huang, Yihua .

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2014, 70 :362-365

[22] Conformational plasticity of molecular chaperones involved in periplasmic and outer membrane protein folding [J].

Mas, Guillaume ;

Hiller, Sebastian .

FEMS MICROBIOLOGY LETTERS, 2018, 365 (13)

[23] Vectorial transport and folding of an autotransporter virulence protein during outer membrane secretion [J].

Junker, Mirco ;

Besingi, Richard N. ;

Clark, Patricia L. .

MOLECULAR MICROBIOLOGY, 2009, 71 (05) :1323-1332

[24] The small molecule nitazoxanide selectively disrupts BAM-mediated folding of the outer membrane usher protein [J].

Psonis, John J. ;

Chahales, Peter ;

Henderson, Nadine S. ;

Rigel, Nathan W. ;

Hoffman, Paul S. ;

Thanassi, David G. .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2019, 294 (39) :14357-14369

[25] Mechanism of outer membrane destabilization by global reduction of protein content [J].

Mikheyeva, Irina V. ;

Sun, Jiawei ;

Huang, Kerwyn Casey ;

Silhavy, Thomas J. .

NATURE COMMUNICATIONS, 2023, 14 (01)

[26] Outer Membrane Protein Folding and Topology from a Computational Transfer Free Energy Scale [J].

Lin, Meishan ;

Gessmann, Dennis ;

Naveed, Hammad ;

Liang, Jie .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2016, 138 (08) :2592-2601

[27] Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs [J].

Bettin, Everton B. ;

Grassmann, Andre A. ;

Dellagostin, Odir A. ;

Gogarten, Johann Peter ;

Caimano, Melissa J. .

SCIENTIFIC REPORTS, 2024, 14 (01)

[28] Cryo-EM structures reveal multiple stages of bacterial outer membrane protein folding [J].

Doyle, Matthew Thomas ;

Jimah, John R. ;

Dowdy, Tyrone ;

Ohlemacher, Shannon, I ;

Larion, Mioara ;

Hinshaw, Jenny E. ;

Bernstein, Harris D. .

CELL, 2022, 185 (07) :1143-+

[29] Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding [J].

Schiffrin, Bob ;

Machin, Jonathan M. ;

Karamanos, Theodoros K. ;

Zhuravleva, Anastasia ;

Brockwell, David J. ;

Radford, Sheena E. ;

Calabrese, Antonio N. .

COMMUNICATIONS BIOLOGY, 2022, 5 (01)

[30] Outer membrane protein BamA-based ELISA differentiates Salmonella-vaccinated chickens from naturally infected chickens [J].

Aribam, Swarmistha Devi ;

Nakayama, Momoko ;

Ogawa, Yohsuke ;

Shimoji, Yoshihiro ;

Eguchi, Masahiro .

JOURNAL OF VETERINARY MEDICAL SCIENCE, 2023, 85 (08) :809-812

← 1 2 3 4 5 →