Proteins in the periplasmic space and outer membrane vesicles of Rhizobium etli CE3 grown in minimal medium are largely distinct and change with growth phase

被引:16
作者
Taboada, Hermenegildo [1 ]
Meneses, Niurka [1 ,2 ,3 ]
Dunn, Michael F. [1 ]
Vargas-Lagunas, Carmen [1 ]
Buchs, Natasha [2 ]
Castro-Mondragon, Jaime A. [4 ]
Heller, Manfred [2 ]
Encarnacion, Sergio [1 ]
机构
[1] Univ Nacl Autonoma Mexico, Ctr Ciencias Genom, Programa Genom Func Procariotes, Cuernavaca 62210, Morelos, Mexico
[2] Univ Bern, Dept Clin Res, Mass Spectrometry & Prote Lab, CH-3010 Bern, Switzerland
[3] Univ Bern, Fac Sci, Dept Chem & Biochem, CH-3010 Bern, Switzerland
[4] Aix Marseille Univ, TAGC, INSERM, UMR S 1090, F-1090 Marseille, France
来源
MICROBIOLOGY-SGM | 2019年 / 165卷 / 06期
关键词
protein secretion; outer membrane vesicles; periplasm; exoproteome; rhizobium-legume interactions; GRAM-NEGATIVE BACTERIA; EXTRACELLULAR PROTEINS; BIOFILM FORMATION; CELL-SURFACE; BAM COMPLEX; I SECRETION; LEGUMINOSARUM; BIOGENESIS; ENVELOPE; EXOPOLYSACCHARIDE;
D O I
10.1099/mic.0.000720
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Rhizobium etli CE3 grown in succinate-ammonium minimal medium (MM) excreted outer membrane vesicles (OMVs) with diameters of 40 to 100 nm. Proteins from the OMVs and the periplasmic space were isolated from 6 and 24 h cultures and identified by proteome analysis. A total of 770 proteins were identified: 73.8 and 21.3% of these occurred only in the periplasm and OMVs, respectively, and only 4.9% were found in both locations. The majority of proteins found in either location were present only at 6 or 24 h: in the periplasm and OMVs, only 24 and 9% of proteins, respectively, were present at both sampling times, indicating a time-dependent differential sorting of proteins into the two compartments. The OMVs contained proteins with physiologically varied roles, including Rhizobium adhering proteins (Rap), polysaccharidases, polysaccharide export proteins, auto-aggregation and adherence proteins, glycosyl transferases, peptidoglycan binding and cross-linking enzymes, potential cell wall-modifying enzymes, porins, multidrug efflux RND family proteins, ABC transporter proteins and heat shock proteins. As expected, proteins with known periplasmic localizations (phosphatases, phosphodiesterases, pyrophosphatases) were found only in the periplasm, along with numerous proteins involved in amino acid and carbohydrate metabolism and transport. Nearly one-quarter of the proteins present in the OMVs were also found in our previous analysis of the R. etli total exproteome of MM-grown cells, indicating that these nanoparticles are an important mechanism for protein excretion in this species.
引用
收藏
页码:638 / 650
页数:13
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