Analysis of the Membrane proteins of an Antarctic Bacterium Pseudomonas Syringae

2011 ◽  
Vol 4 ◽  
pp. PRI.S5383 ◽  
Author(s):  
M.V. Jagannadham ◽  
S. Saranya
Keyword(s):  
Comparative Analysis ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Pseudomonas Syringae ◽  
Cold Adaptation ◽  
Outer Membrane Proteins ◽  
Protein Preparation ◽  
Preparation Methods ◽  
Outer Membranes ◽  
Antarctic Bacterium

The proteins of an Antarctic bacterium Pseudomonas syringae Lz4W, identified earlier by different membrane protein preparation methods, were combined together and the redundant identities removed. In total, 1479 proteins including 148 outer membrane proteins from this bacterium were predicted by the algorithm PSORTb3.0. A detailed analysis on their subcellular localization was undertaken which was determined using TMHMM, TMB-hunt and BOMP. A comparison of PSORTb predicted outer membrane proteins with BOMP, revealed that most of the proteins predicted by the former, contained β–barrels in the outer membranes. A comparative analysis of PSORTb, TMHMM and TMB-hunt reveals that most of the outer membranes proteins of this bacterium could be identified using this approach. Thus, by using a combination of biochemical and different bioinformatics algorithms, the membrane proteins of P. syringae are analyzed. In particular, PSORTb results are compared and supported by other algorithms, to improve the strength of OM proteins prediction. Several proteins, having an important role in cold adaptation of the organism, could also be identified.

scholarly journals A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria

2016 ◽  
Vol 291 (32) ◽  
pp. 16720-16729 ◽  
Author(s):  
Yan Wang ◽  
Rui Wang ◽  
Feng Jin ◽  
Yang Liu ◽  
Jiayu Yu ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Outer Membranes

scholarly journals Fate of Predator and Prey Proteins during Growth of Bdellovibrio bacteriovorus on Escherichia coli and Pseudomonas syringae Prey

2005 ◽  
Vol 187 (1) ◽  
pp. 329-335 ◽  
Author(s):  
Gilli Barel ◽  
Alexandra Sirota ◽  
Hanne Volpin ◽  
Edouard Jurkevitch
Keyword(s):  
Escherichia Coli ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Pseudomonas Syringae ◽  
Outer Membrane Proteins ◽  
Cell Fraction ◽  
Two Dimensional ◽  
Protein Distribution ◽  
Bdellovibrio Bacteriovorus ◽  
Cell Envelopes

ABSTRACT A two-dimensional electrophoretic analysis of protein distribution followed by identification of selected proteins by mass spectrometry was performed on fresh bdellovibrio cultures containing attack phase cells of the predatory bacterium Bdellovibrio bacteriovorus strain 109J-1 and the remains of an Escherichia coli or a Pseudomonas syringae pv. tomato prey. Cleavage of the peptidoglycan-associated outer membrane proteins (OMPs) OmpA in E. coli and OprF in P. syringae occurred in both prey. The tryptic peptides obtained from the cleavage products of OmpA and OprF were all located within the 19-kDa pronase-resistant N-terminal parts of the corresponding proteins. The predator cell fraction was separated from the prey ghosts in fresh bdellovibrio cultures by centrifugation on a Percoll-sucrose cushion. Proteins from each fraction were separated by two-dimensional electrophoresis and identified by mass spectrometric analysis. As no prey OMP could be detected in the predator cell fraction, it was concluded that prey OMPs are not transferred to the predator, as had been suggested previously. However, a protein from the predator was found bound to ghost cell envelopes. This protein may correspond to a protein earlier suggested to be associated with the prey outer or cytoplasmic membranes. Along with recently described polypeptides from B. bacteriovorus strains 100 and 114, it forms a new family of putative outer membrane proteins.

Comparative analysis of the main outer membrane proteins of Brucella in the diagnosis of brucellosis

2021 ◽  
Vol 560 ◽  
pp. 126-131
Author(s):  
Qiongqiong Bai ◽  
Han Li ◽  
Xiling Wu ◽  
Jihong Shao ◽  
Mingjun Sun ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins

scholarly journals Omp85Tt from Thermus thermophilus HB27: an Ancestral Type of the Omp85 Protein Family

2008 ◽  
Vol 190 (13) ◽  
pp. 4568-4575 ◽  
Author(s):  
Jutta Nesper ◽  
Alexander Brosig ◽  
Philippe Ringler ◽  
Geetika J. Patel ◽  
Shirley A. Müller ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Single Channel ◽  
Cell Envelope ◽  
Thermus Thermophilus ◽  
Outer Membrane Proteins ◽  
Thermophilic Bacterium ◽  
Outer Membranes ◽  
Β Sheet ◽  
Ancestral Type

ABSTRACT Proteins belonging to the Omp85 family are involved in the assembly of β-barrel outer membrane proteins or in the translocation of proteins across the outer membrane in bacteria, mitochondria, and chloroplasts. The cell envelope of the thermophilic bacterium Thermus thermophilus HB27 is multilayered, including an outer membrane that is not well characterized. Neither the precise lipid composition nor much about integral membrane proteins is known. The genome of HB27 encodes one Omp85-like protein, Omp85Tt, representing an ancestral type of this family. We overexpressed Omp85Tt in T. thermophilus and purified it from the native outer membranes. In the presence of detergent, purified Omp85Tt existed mainly as a monomer, composed of two stable protease-resistant modules. Circular dichroism spectroscopy indicated predominantly β-sheet secondary structure. Electron microscopy of negatively stained lipid-embedded Omp85Tt revealed ring-like structures with a central cavity of ∼1.5 nm in diameter. Single-channel conductance recordings indicated that Omp85Tt forms ion channels with two different conducting states, characterized by conductances of ∼0.4 nS and ∼0.65 nS, respectively.

scholarly journals A Topology Structure Based Outer Membrane Proteins Segment Alignment Method

2013 ◽  
Vol 2013 ◽  
pp. 1-10 ◽  
Author(s):  
Han Wang ◽  
Bo Liu ◽  
Pingping Sun ◽  
Zhiqiang Ma
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Transmembrane Proteins ◽  
Structure Alignment ◽  
Spatial Structures ◽  
Alignment Method ◽  
Outer Membranes ◽  
Novel Method ◽  
Segment Orientation

Outer membrane proteins (OMPs) are transmembrane proteins (TMPs) located in outer membranes. These proteins perform diverse biochemical functions and have immediate medical relevance, so that their spatial structures are important for studying. But the special physicochemical properties of OMP make it hard to obtain their structures experimentally. For the purpose of predicting OMP structures, discriminating OMPs and aligning their sequences to native structures are indispensable steps. We developed a novel method OMSA (Outer Membrane Segment Alignment), which implemented both steps in one program. OMSA integrates OMP-specific topology features to implement a sequence-to-structure alignment, for example, segment type and segment orientation, while a segment-dependent gap penalty model is employed to improve the alignment. Compared to peer top-leading methods, OMSA achieved higher accuracy in both OMP discrimination and alignment, which may further improve OMP structure studying.

Sign in / Sign up

Export Citation Format

Share Document