scholarly journals Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons

1992 ◽  
Vol 284 (2) ◽  
pp. 469-476 ◽  
Author(s):  
M E Cheetham ◽  
J P Brion ◽  
B H Anderton
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Human Brain ◽  
Atp Hydrolysis ◽  
Sequence Similarity ◽  
Polyclonal Antiserum ◽  
Cdna Clones ◽  
Expression Library ◽  
Dnaj Protein ◽  
Protein Complex Dissociation

The bacterial heat-shock protein DnaJ has been implicated in protein folding and protein complex dissociation. The DnaJ protein interacts with the prokaryotic analogue of Hsp70, DnaK, and accelerates the rate of ATP hydrolysis by DnaK. Several yeast homologues of DnaJ, with different proposed subcellular localizations and functions, have recently been isolated and are the only eukaryotic forms of DnaJ so far described. We have isolated cDNAs corresponding to two alternatively spliced transcripts of a novel human gene, HSJ1, which show sequence similarity to the bacterial DnaJ protein and the yeast homologues. The cDNA clones were isolated from a human brain-frontal-cortex expression library screened with a polyclonal antiserum raised to paired-helical-filament (PHF) proteins isolated from extracts of the brains of patients suffering from Alzheimer's disease. The similarity between the predicted human protein sequences and the bacterial and yeast proteins is highest at the N-termini, this region also shows a limited similarity to viral T-antigens and is a possible common motif involved in the interaction with DnaK/Hsp70. Northern-blot analysis has shown that human brain contains higher levels of mRNA for the DnaJ homologue than other tissues examined, and hybridization studies with riboprobes in situ show a restricted pattern of expression of the mRNA within the brain, with neuronal layers giving the strongest signal. These findings suggest that the DnaJ-DnaK (Hsp70) interaction is general to eukaryotes and, indeed, to higher organisms.

scholarly journals Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38)

1990 ◽  
Vol 270 (1) ◽  
pp. 97-102 ◽  
Author(s):  
J P Luzio ◽  
B Brake ◽  
G Banting ◽  
K E Howell ◽  
P Braghetta ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Integral Membrane Protein ◽  
Polyclonal Antiserum ◽  
Cdna Expression Library ◽  
Cdna Clones ◽  
Expression Library ◽  
Trans Golgi Network ◽  
Sequencing And Expression ◽  
Novel Strategy ◽  
Golgi Network

Organelle-specific integral membrane proteins were identified by a novel strategy which gives rise to monospecific antibodies to these proteins as well as to the cDNA clones encoding them. A cDNA expression library was screened with a polyclonal antiserum raised against Triton X-114-extracted organelle proteins and clones were then grouped using antibodies affinity-purified on individual fusion proteins. The identification, molecular cloning and sequencing are described of a type 1 membrane protein (TGN38) which is located specifically in the trans-Golgi network.

scholarly journals Alterations in inducible 72-kDa heat shock protein and the chaperone cofactor BAG-1 in human brain after head injury

2003 ◽  
Vol 84 (3) ◽  
pp. 514-521 ◽  
Author(s):  
Neal A. Seidberg ◽  
Robert S. B. Clark ◽  
Xiaopeng Zhang ◽  
Yichen Lai ◽  
Minzhi Chen ◽  
...  
Keyword(s):  
Head Injury ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Human Brain

scholarly journals Exercise induces the release of heat shock protein 72 from the human brain in vivo

2004 ◽  
Vol 9 (3) ◽  
pp. 276 ◽  
Author(s):  
G. I. Lancaster ◽  
K. Møller ◽  
B. Nielsen ◽  
N. H. Secher ◽  
M. A. Febbraio ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Human Brain ◽  
Heat Shock Protein 72

scholarly journals The Unique Chaperone Operon of Thermotoga maritima: Cloning and Initial Characterization of a Functional Hsp70 and Small Heat Shock Protein

1999 ◽  
Vol 181 (14) ◽  
pp. 4237-4244 ◽  
Author(s):  
Edward T. Michelini ◽  
Gregory C. Flynn
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Chaperones ◽  
Atp Hydrolysis ◽  
Thermotoga Maritima ◽  
Small Heat Shock Protein ◽  
Chaperone Protein ◽  
Operon Organization

ABSTRACT The hyperthermophilic eubacterium Thermotoga maritimapossesses an operon encoding an Hsp70 molecular chaperone protein and a protein with meaningful homology to the small heat shock protein family of chaperones. This represents the first demonstrated co-operon organization for these two important classes of molecular chaperones. We have cloned and initially characterized these proteins as functional chaperones in vitro: the Hsp70 is capable of ATP hydrolysis and substrate binding, and the small heat shock protein can suppress protein aggregation and stably bind a refolding-competent substrate. In addition, the primary sequence of the Hsp70 is used to infer the phylogenetic relationships of T. maritima, one of the deepest-branching eubacteria known.

Heat shock protein (hsx70) mRNA expression in human brain: effects of neurodegenerative disease and agonal state

1993 ◽  
Vol 19 (1) ◽  
pp. 10-21 ◽  
Author(s):  
P. J. Harrison ◽  
A. W. Procter ◽  
T. Exworthy ◽  
G. W. Roberts ◽  
A. Najlerahim ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Human Brain ◽  
Neurodegenerative Disease ◽  
Mrna Expression ◽  
Agonal State

scholarly journals Laminin in the male germ cells of Drosophila.

1992 ◽  
Vol 119 (4) ◽  
pp. 977-988 ◽  
Author(s):  
F Wang ◽  
M Hanske ◽  
K Miedema ◽  
G Klein ◽  
P Ekblom ◽  
...  
Keyword(s):  
Germ Cells ◽  
Polyclonal Antibodies ◽  
Sequence Similarity ◽  
Primary Spermatocyte ◽  
Complete Sequence ◽  
Polyclonal Antiserum ◽  
Cdna Expression Library ◽  
Expression Library ◽  
Male Germ Cells

To study genes that may be crucial for the male germ cell development of Drosophila we screened a cDNA expression library with a polyclonal antiserum against testis proteins of Drosophila hydei. We identified a cDNA fragment that exhibited a complete sequence similarity with the cDNA of the laminin B2 chain, an important component of the extracellular matrix. Transcripts of laminin B2 were detected in the RNA of male germ cells with the polymerase chain reaction and by in situ hybridization. We studied the reaction of different polyclonal antibodies including those against a Drosophila laminin B2-lac fusion protein, the entire Drosophila laminin complex, or against the mouse laminin complex and against laminin A and B1 chains with specific structures in developing male germ cells of Drosophila. Antigenic sites against laminin B2 were found in the lampbrush loops in primary spermatocyte nuclei, in nuclei of spermatids, and in heads of spermatozoa. The axonemes of elongating spermatids react with antibodies against the Drosophila laminin B1, B2 and laminin A chains. The possible biological functions of the laminin in the male germ cells of Drosophila are discussed.

scholarly journals Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90

2012 ◽  
Vol 44 (4) ◽  
pp. 300-306 ◽  
Author(s):  
Jian Li ◽  
Lihua Sun ◽  
Chunyan Xu ◽  
Feng Yu ◽  
Huan Zhou ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Atp Hydrolysis ◽  
Heat Shock Protein 90 ◽  
Human Heat Shock Protein

Developmental changes of heat shock protein 73 in human brain

1995 ◽  
Vol 86 (1-2) ◽  
pp. 180-186 ◽  
Author(s):  
Mitsuhiro Kato ◽  
Masashi Mizuguchi ◽  
Sachio Takashima
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Human Brain ◽  
Developmental Changes

ArHsp21, a developmentally regulated small heat-shock protein synthesized in diapausing embryos of Artemia franciscana

2008 ◽  
Vol 411 (3) ◽  
pp. 605-611 ◽  
Author(s):  
Zhijun Qiu ◽  
Thomas H. MacRae
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Citrate Synthase ◽  
Sequence Similarity ◽  
Single Gene ◽  
Small Heat Shock Protein ◽  
Subtractive Hybridization ◽  
Artemia Franciscana ◽  
Induced Aggregation

Embryos of the crustacean, Artemia franciscana, undergo alternative developmental pathways, producing either larvae or encysted embryos (cysts). The cysts enter diapause, characterized by exceptionally high resistance to environmental stress, a condition thought to involve the sHSP (small heat-shock protein), p26. Subtractive hybridization has revealed another sHSP, termed ArHsp21, in diapause-destined Artemia embryos. ArHsp21 shares sequence similarity with p26 and sHSPs from other organisms, especially in the α-crystallin domain. ArHsp21 is the product of a single gene and its synthesis occurred exclusively in diapause-destined embryos. Specifically, ArHsp21 mRNA appeared 2 days post-fertilization, followed 1 day later by the protein, and then increased until embryo release at day 5. No ArHsp21 protein was detected in embryos developing directly into larvae, although there was a small amount of mRNA at 3 days post-fertilization. The protein was degraded during post-diapause development and had disappeared completely from second instar larvae. ArHsp21 formed large oligomers in encysted embryos and transformed bacteria. When purified from bacteria, ArHsp21 functioned as a molecular chaperone in vitro, preventing heat-induced aggregation of citrate synthase and reduction-driven denaturation of insulin. Sequence characteristics, synthesis patterns and functional properties demonstrate clearly that ArHsp21 is an sHSP able to chaperone other proteins and contribute to stress tolerance during diapause. As such, ArHsp21 would augment p26 chaperone activity and it may also possess novel activities that benefit Artemia embryos exposed to stress.

Sign in / Sign up

Export Citation Format

Share Document