scholarly journals Molecular Characterization of Radial Spoke Subcomplex Containing Radial Spoke Protein 3 and Heat Shock Protein 40 in Sperm Flagella of the AscidianCiona intestinalis

2005 ◽  
Vol 16 (2) ◽  
pp. 626-636 ◽  
Author(s):  
Yuhkoh Satouh ◽  
Potturi Padma ◽  
Toshifusa Toda ◽  
Nori Satoh ◽  
Hiroyuki Ide ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Sequence Similarity ◽  
Protein A ◽  
Gel Filtration ◽  
Peptide Mass Fingerprinting ◽  
Distal Portion ◽  
Radial Spoke ◽  
Flight Mass Spectrometry ◽  
Peptide Mass

Members of the heat-shock protein (HSP)40 regulate the protein folding activity of HSP70 proteins and help the functional specialization of this molecular chaperone system in various types of cellular events. We have recently identified Hsp40 as a component of flagellar axoneme in the ascidian Ciona intestinalis, suggesting a correlation between Hsp40 related chaperone system and flagellar function. In this study, we have found that Ciona 37-kDa Hsp40 is extracted from KCl-treated axonemes with 0.5 M KI solution and comigrates with radial spoke protein (RSP)3 along with several proteins as a complex through gel filtration and ion exchange columns. Peptide mass fingerprinting with matrix-assisted laser desorption ionization/time of flight/mass spectrometry revealed that other proteins in the complex include a homolog of sea urchin spokehead protein (homolog of RSP4/6), a membrane occupation and recognition nexus repeat protein with sequence similarity with meichroacidin, and a functionally unknown 33-kDa protein. A spoke head protein, LRR37, is not included in the complex, suggesting that the complex constructs the stalk of radial spoke. Immunoelectron microscopy indicates that Hsp40 is localized in the distal portion of spoke stalk, possibly at the junction between spoke head and the stalk.

The 90 000 dalton heat shock protein, a lot of smoke but no function as yet

1989 ◽  
Vol 67 (11-12) ◽  
pp. 749-750 ◽  
Author(s):  
Boyd Hardesty ◽  
Gisela Kramer
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein A

Increased expression of collagen-binding heat shock protein 47 in murine bleomycin-induced pneumopathy

2003 ◽  
Vol 285 (4) ◽  
pp. L957-L963 ◽  
Author(s):  
Hiroshi Ishii ◽  
Hiroshi Mukae ◽  
Tomoyuki Kakugawa ◽  
Tetsuji Iwashita ◽  
Hideyuki Kaida ◽  
...  
Keyword(s):  
Heat Shock ◽  
Pulmonary Fibrosis ◽  
Heat Shock Protein ◽  
Smooth Muscle Actin ◽  
Protein A ◽  
Immunohistochemical Analysis ◽  
Rt Pcr ◽  
Heat Shock Protein 47 ◽  
Positive Type ◽  
Fibrotic Process

The 47-kDa heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that has been shown to play a major role during the processing and/or secretion of procollagen. Expression of HSP47 has been reported to increase in parallel with expression of collagens during the progression of various fibrosis models. The aim of the present study was to investigate the association between HSP47 expression and collagen accumulation in bleomycin (BLM)-induced murine fibrosis. We investigated the expression of HSP47 protein and mRNA using immunohistochemical analysis and semi-quantitative RT-PCR in murine BLM-induced pulmonary fibrosis. Immunohistochemical analysis showed that higher expression of HSP47 protein was present in BLM-induced pulmonary fibrosis compared with controls. HSP47 was localized predominantly in α-smooth muscle actin-positive myofibroblasts, F4/80 negative, surfactant protein-A-positive type II pneumocytes, and F4/80-positive macrophages. RT-PCR also demonstrated an increase of HSP47 mRNA expression in BLM-treated lungs. Moreover, the relative amounts of HSP47 mRNA correlated significantly with the lung hydroxyproline content as an indicator of pulmonary fibrosis in BLM-treated lungs ( r = 0.406, P <0.05). Our results suggest that these cells may play a role in the fibrotic process of BLM-treated lungs through upregulation of HSP47.

scholarly journals The surface (S)-layer gene cspB of Corynebacterium glutamicum is transcriptionally activated by a LuxR-type regulator and located on a 6 kb genomic island absent from the type strain ATCC 13032

Microbiology ◽  
2006 ◽  
Vol 152 (4) ◽  
pp. 923-935 ◽  
Author(s):  
Nicole Hansmeier ◽  
Andreas Albersmeier ◽  
Andreas Tauch ◽  
Thomas Damberg ◽  
Robert Ros ◽  
...  
Keyword(s):  
Corynebacterium Glutamicum ◽  
Affinity Purification ◽  
Regulatory Protein ◽  
Direct Repeat ◽  
Peptide Mass Fingerprinting ◽  
Gene Encoding ◽  
Force Microscopy ◽  
Flight Mass Spectrometry ◽  
Peptide Mass ◽  
Rapid Amplification

The surface (S)-layer gene region of the Gram-positive bacterium Corynebacterium glutamicum ATCC 14067 was identified on fosmid clones, sequenced and compared with the genome sequence of C. glutamicum ATCC 13032, whose cell surface is devoid of an ordered S-layer lattice. A 5·97 kb DNA region that is absent from the C. glutamicum ATCC 13032 chromosome was identified. This region includes cspB, the structural gene encoding the S-layer protomer PS2, and six additional coding sequences. PCR experiments demonstrated that the respective DNA region is conserved in different C. glutamicum wild-type strains capable of S-layer formation. The DNA region is flanked by a 7 bp direct repeat, suggesting that illegitimate recombination might be responsible for gene loss in C. glutamicum ATCC 13032. Transfer of the cloned cspB gene restored the PS2− phenotype of C. glutamicum ATCC 13032, as confirmed by visualization of the PS2 proteins by SDS-PAGE and imaging of ordered hexagonal S-layer lattices on living C. glutamicum cells by atomic force microscopy. Furthermore, the promoter of the cspB gene was mapped by 5′ rapid amplification of cDNA ends PCR and the corresponding DNA fragment was used in DNA affinity purification assays. A 30 kDa protein specifically binding to the promoter region of the cspB gene was purified. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry and peptide mass fingerprinting of the purified protein led to the identification of the putative transcriptional regulator Cg2831, belonging to the LuxR regulatory protein family. Disruption of the cg2831 gene in C. glutamicum resulted in an almost complete loss of PS2 synthesis. These results suggested that Cg2831 is a transcriptional activator of cspB gene expression in C. glutamicum.

scholarly journals A Novel Bipartite Double-Stranded RNA Mycovirus from the White Root Rot Fungus Rosellinia necatrix: Molecular and Biological Characterization, Taxonomic Considerations, and Potential for Biological Control

2009 ◽  
Vol 83 (24) ◽  
pp. 12801-12812 ◽  
Author(s):  
Sotaro Chiba ◽  
Lakha Salaipeth ◽  
Yu-Hsin Lin ◽  
Atsuko Sasaki ◽  
Satoko Kanematsu ◽  
...  
Keyword(s):  
Biological Control ◽  
Root Rot ◽  
Sequence Similarity ◽  
Peptide Mass Fingerprinting ◽  
Dsrna Virus ◽  
Rosellinia Necatrix ◽  
Virus Family ◽  
White Root Rot ◽  
Double Stranded Rna ◽  
Peptide Mass

ABSTRACT White root rot, caused by the ascomycete Rosellinia necatrix, is a devastating disease worldwide, particularly in fruit trees in Japan. Here we report on the biological and molecular properties of a novel bipartite double-stranded RNA (dsRNA) virus encompassing dsRNA-1 (8,931 bp) and dsRNA-2 (7,180 bp), which was isolated from a field strain of R. necatrix, W779. Besides the strictly conserved 5′ (24 nt) and 3′ (8 nt) terminal sequences, both segments show high levels of sequence similarity in the long 5′ untranslated region of approximately 1.6 kbp. dsRNA-1 and -2 each possess two open reading frames (ORFs) named ORF1 to -4. Although the protein encoded by 3′-proximal ORF2 on dsRNA-1 shows sequence identities of 22 to 32% with RNA-dependent RNA polymerases from members of the families Totiviridae and Chrysoviridae, the remaining three virus-encoded proteins lack sequence similarities with any reported mycovirus proteins. Phylogenetic analysis showed that the W779 virus belongs to a separate clade distinct from those of other known mycoviruses. Purified virions ∼50 nm in diameter consisted of dsRNA-1 and -2 and a single major capsid protein of 135 kDa, which was shown by peptide mass fingerprinting to be encoded by dsRNA-1 ORF1. We developed a transfection protocol using purified virions to show that the virus was responsible for reduction of virulence and mycelial growth in several host strains. These combined results indicate that the W779 virus is a novel bipartite dsRNA virus with potential for biological control (virocontrol), named Rosellinia necatrix megabirnavirus 1 (RnMBV1), that possibly belongs to a new virus family.

IS HEAT SHOCK PROTEIN A POTENTIAL PROTECTIVE MECHANISM AGAINST ISCHEMIA-REPERFUSION INJURY?

1999 ◽  
Vol 103 (1) ◽  
pp. 336-337 ◽  
Author(s):  
Sean Lille ◽  
Ching-Yuan Su ◽  
Michael Neumeister ◽  
Robert C. Russell ◽  
Chen-Ching Lai
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Reperfusion Injury ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Protein A ◽  
Protective Mechanism

scholarly journals A Histidine-rich and Cysteine-rich Metal-binding Domain at the C Terminus of Heat Shock Protein A fromHelicobacter pylori

2008 ◽  
Vol 283 (22) ◽  
pp. 15142-15151 ◽  
Author(s):  
Shujian Cun ◽  
Hongyan Li ◽  
Ruiguang Ge ◽  
Marie C. M. Lin ◽  
Hongzhe Sun
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Metal Binding ◽  
Protein A ◽  
Binding Domain ◽  
C Terminus ◽  
Metal Binding Domain

scholarly journals Chemical modifications of a recombinant bovine stress-inducible 70 kDa heat-shock protein (Hsp70) mimics Hsp70 isoforms from tissues

1995 ◽  
Vol 305 (1) ◽  
pp. 197-203 ◽  
Author(s):  
J A Gutierrez ◽  
V Guerriero
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Expression System ◽  
Protein A ◽  
Two Dimensional Gel Electrophoresis ◽  
Calculated Molecular Mass ◽  
Reading Frame ◽  
Heat Shock Protein Hsp70 ◽  
Bovine Skeletal Muscle

A cDNA clone for the stress-inducible 70 kDa heat-shock protein (Hsp70) has been isolated from a bovine skeletal-muscle cDNA library. This mRNA encodes a protein with a calculated molecular mass of 70250 Da. The cDNA has one continuous open reading frame capable of encoding a 641-amino-acid protein. Expression of this cDNA in a bacterial expression system produced a protein with a mobility identical with that of the inducible Hsp70 protein from bovine skeletal muscle as determined by SDS/PAGE. Two-dimensional gel electrophoresis demonstrated this protein to have focusing properties identical with that of a minor isoform from bovine skeletal muscle. Upon carbamylation of this bacterially expressed protein, a train of charged proteins with charge differences of -1 were produced. These carbamylated proteins were shown to have similar focusing mobilities to the Hsp70 isoforms isolated from bovine skeletal muscle. These results demonstrate the identification of a skeletal-muscle inducible Hsp70 gene and suggest that the presence of multiple Hsp70 isoforms may be the product of post-translational modifications to the Hsp70 proteins.

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