Crystallization and preliminary X-ray analysis of FliJ, a cytoplasmic component of the flagellar type III protein-export apparatus fromSalmonellasp.

The > 40-keV solar-flare electrons observed by the IMP III and Mariner IV satellites are shown to be closely correlated with solar radio and X-ray burst emission. In particular, intense type III radio bursts are observed to accompany solar electron-event flares. The energies of the electrons, the total number of electrons, and the size of the electron source at the sun can be inferred from radio observations. The characteristics of the electrons observed in interplanetary space are consistent with these radio observations. Therefore these electrons are identified as the exciting agents of the type III emission. It has been noted that the radio and X-ray bursts are part of the flash phase of flares. The observations indicate that a striking feature of the flash phase is the production of electrons of 10–100 keV energies.

Download Full-text

Coronal Hard X‐Ray Emission Associated with Radio Type III Bursts

The Astrophysical Journal ◽

10.1086/588549 ◽

2008 ◽

Vol 681 (1) ◽

pp. 644-649 ◽

Cited By ~ 26

Author(s):

Säm Krucker ◽

P. Saint‐Hilaire ◽

S. Christe ◽

S. M. White ◽

A. D. Chavier ◽

...

Keyword(s):

X Ray ◽

Type Iii

Download Full-text

2P256 Physicochemical and structural analysis of mutant FlhA, a subunit protein of the flagellar type III protein export apparatus of Salmonella(39. Cell motility,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

Seibutsu Butsuri ◽

10.2142/biophys.46.s359_4 ◽

2006 ◽

Vol 46 (supplement2) ◽

pp. S359

Author(s):

Masafumi Shimada ◽

Yumiko Saijyo-Hamano ◽

Yukio Furukawa ◽

Thoru Minamino ◽

Katsumi Imada ◽

...

Keyword(s):

Structural Analysis ◽

Cell Motility ◽

Poster Session ◽

Protein Export ◽

Subunit Protein ◽

Type Iii ◽

Meeting Program ◽

A Subunit

Download Full-text

Crystallization and preliminary X-ray analysis of the FliH–FliI complex responsible for bacterial flagellar type III protein export

Acta Crystallographica Section F Structural Biology and Crystallization Communications ◽

10.1107/s1744309112030801 ◽

2012 ◽

Vol 68 (11) ◽

pp. 1311-1314 ◽

Cited By ~ 2

Author(s):

Yumiko Uchida ◽

Tohru Minamino ◽

Keiichi Namba ◽

Katsumi Imada

Keyword(s):

Self Assembly ◽

Specific Protein ◽

Protein Export ◽

Orthorhombic Space Group ◽

X Ray ◽

Cell Parameters ◽

Peg 400 ◽

Diffusion Technique ◽

Flagellar Proteins ◽

Soluble Components

The bacterial flagellar proteins are translocated into the central channel of the flagellum by a specific protein-export apparatus for self-assembly at the distal growing end. FliH and FliI are soluble components of the export apparatus and form an FliH2–FliI heterotrimer in the cytoplasm. FliI is an ATPase and the FliH2–FliI complex delivers export substrates from the cytoplasm to an export gate made up of six integral membrane proteins of the export apparatus. In this study, an FliHCfragment consisting of residues 99–235 was co-purified with FliI and the FliHC2–FliI complex was crystallized. Crystals were obtained using the hanging-drop vapour-diffusion technique with PEG 400 as a precipitant. The crystals belonged to the orthorhombic space groupP212121, with unit-cell parametersa= 133.7,b= 147.3,c= 164.2 Å, and diffracted to 3.0 Å resolution.

Download Full-text