Post by skyship on Jul 4, 2009 2:22:07 GMT -5
One and the same? hope not. But......?
I. from this loaded link:
www.palaeos.com/Bacteria/Lists/Glossary/Gloss.html#DnaK
..."DnaK: a bacterial chaperonin homologous to the Hsp70 of eukaryotes. DnaK works in tandem with DnaJ and GrpE to accomplish ATP-dependant folding of polypeptides. DnaK is a heat shock protein. However, when not operating under heat shock conditions, DnaK is also present and is involved in the degradation of σ32, an RNA polymerase regulator which detects the promoter sites for transcription of RNA coding for heat shock proteins"...
===========
II.Chaperonin
,,,"Chaperonin: any of a class of ATP-dependant (i.e. they need chemical energy to do the job) proteins which are responsible for folding polypeptides into the correct conformation. As anyone who has been confronted with a spool of ribbon and a pile of presents knows, the ribbon will not fold itself into an appropriately decorative conformation. Even though the desired conformation is stable and energetially favorable, the ribbon needs energetic guidance to attain this state within some biologically relevant timescale. This is the function of chaperonins. They are composed of two oir more doughnut-shaped subunits. Chaperonins also have a limited ability to "repair" proteins which have been incorrectly folded. Class I chaperonins are chaperonins closely related to the E. coli GroEL protein, and are sometimes referred to as GroE chaperonins. The holoenzyme is composed of two heptameric subunits and works in concert with a helper Hsp 10 protein (GroES). Class I chaperonins are found in Eubacteria, mitochondria, and chloroplasts. Class II chaperonins, or TCP1 proteins include both the thermosomes or TF55 proteins of Archaea and the CCT proteins of eukaryotes. The eukaryotic species are composed of two octameric rings, while thermosomes may have either 8 or 9-member rings. Class II chaperonins do not have a helper protein. Class II chaperonins are very closely related to Class I chaperonins by structure, but not by sequence. For more information, see Pieces: GroEL.",,,,,,
III. DnaK from DnaJ and GrpE:
Link:
tinyurl.com/ml9bt2
www-nmr.cabm.rutgers.edu/photogallery/proteins
/htm/page19.htm
....."DnaJ is a heat shock induced protein from the bacterium Escherichia coli which is under control of thr htpr regulatory protein. DnaJ interacts with the chaperone Hsp70-like DnaK protein to disassemble a protein complex found at a phage lambda's origin of replication (ORI). Also, DnaJ with the joint effort of GrpE stimulates the ATPase activity of DnaK. DnaJ, DnaK, and GrpE are all involved in a variety of biological processes: protein folding and transport, cell survival at high temperatures, negative autoregulation of the heat shock response, and the replication of bacteriophage lambda and other plasmids.
DnaJ is 376 amino acid residues long. However, the N-terminal amino acid residues 2-108 retain much of the entire protein's biological function and capabilities. Within this region is the J domain, comprised of residues 2-72. It consists of four alpha helices: 1=Blue, 2=Green, 3=Pink, and 4=Gold. Helices 2 and 3 are in an antiparallel fashion, and in the center of this polypeptide fragment is a conserved hydrophobic core.".......
=================
IV. GrpE
Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J; , Science 1997;276:431-435.: Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. PUBMED:9103205
Interpro entry IPR000740
Molecular chaperones are a diverse family of proteins that function to protect proteins in the intracellular milieu from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-terminal ATP-hydrolysing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. In prokaryotes the grpE protein. Dimeric GrpE is the co-chaperone for DnaK, and acts as a nucleotide exchange factor, stimulating the rate of ADP release 5000-fold PUBMED:8280473.[/u] DnaK is itself a weak ATPase; ATP hydrolysis by DnaK is stimulated by its interaction with another co-chaperone, DnaJ. Thus the co-chaperones DnaJ and GrpE are capable of tightly regulating the nucleotide-bound and substrate-bound state of DnaK in ways that are necessary for the normal housekeeping functions and stress-related functions of the DnaK molecular chaperone cycle.
The X-ray crystal structure of GrpE in complex with the ATPase domain of DnaK revealed that GrpE is an asymmetric homodimer, bent in a manner that favours extensive contacts with only one DnaKATPase monomer PUBMED:15136046. GrpE does not actively compete for the atomic positions occupied by the nucleotide. GrpE and ADP mutually reduce one another's affinity for DnaK 200-fold, and ATP instantly dissociates GrpE from DnaK."
V. Sigma 32: it is an rpoH gene product.
links:
www.wikigenes.org/e/gene/e/947970.html
tinyurl.com/l6h3mp
www.ihop-net.org/UniPub/iHOP/gs/171051.html?
list=1&page=1
Note the different proteins affiliated with.
Here is what the Sigma H reacts to and notice all in e-coli,
this was the first organism they used as a model, now if it is
a model, might they just be using it to incorporate the dimers
(artificial) proteins into us. If there is problems with the polypeptide
then herein is the first use of this catianic artificial polymer into
live peptides.?.......
VI. Dimeric GrpE
VII. Llamda Bacteriophage
www.pubmedcentral.nih.gov/articlerender.fcgi?artid=390449
Finally found Janelle Farms again........will check them out. affiliated
with HHMI How Hughs Med Institute. and others......They could
be trying to fix this or carry on as usual. Incidentally heat shock
proteins are supposed to be what they call "immortal genes", but,
in my mind they are artificial peptides, proteins, being integrated
in. Do you ever notice that the fibers do not seem real, like they
have an artificial non degrading, non dissolving (insoluable) factor
to them? In otherwords, they can't be burned, do not dissolve,
only when dry or out of the medium, our mucus, our plasma, our
blood, etc. once out of the source they fall apart. Seems prions
are like that as well, seems prions have something to do with
the unfolding and folding as well.
So, DnaK is a CHAPERONIN homologenous to HSP 70(heat shock protein 70) of eukaryotes (mulicelled) ??KDNA?
Works with DnaJ (e-coli), and GrpE (from prokaryote(directed
constructed evolution,) ADP-dependent, folding of polypeptide.
They fused the prokaryote to the eukaryote in this novel
creation.
DnaK is a heat shock protein.
when not in heat shock mode degrades alpha 32? .."an RNA polymerase regulator which detects the promoter sites for transcription of RNA coding for heat shock proteins"
sigma 32 is a rpoH,
GrpE and Dimeric GrpE
DIMERS ARE MAN MADE..................
okay the Lamda phage is what we need to look at and
start with
DnaA.......THE INITIATION Protein O and protein P
next post.
skyship
I. from this loaded link:
www.palaeos.com/Bacteria/Lists/Glossary/Gloss.html#DnaK
..."DnaK: a bacterial chaperonin homologous to the Hsp70 of eukaryotes. DnaK works in tandem with DnaJ and GrpE to accomplish ATP-dependant folding of polypeptides. DnaK is a heat shock protein. However, when not operating under heat shock conditions, DnaK is also present and is involved in the degradation of σ32, an RNA polymerase regulator which detects the promoter sites for transcription of RNA coding for heat shock proteins"...
===========
II.Chaperonin
,,,"Chaperonin: any of a class of ATP-dependant (i.e. they need chemical energy to do the job) proteins which are responsible for folding polypeptides into the correct conformation. As anyone who has been confronted with a spool of ribbon and a pile of presents knows, the ribbon will not fold itself into an appropriately decorative conformation. Even though the desired conformation is stable and energetially favorable, the ribbon needs energetic guidance to attain this state within some biologically relevant timescale. This is the function of chaperonins. They are composed of two oir more doughnut-shaped subunits. Chaperonins also have a limited ability to "repair" proteins which have been incorrectly folded. Class I chaperonins are chaperonins closely related to the E. coli GroEL protein, and are sometimes referred to as GroE chaperonins. The holoenzyme is composed of two heptameric subunits and works in concert with a helper Hsp 10 protein (GroES). Class I chaperonins are found in Eubacteria, mitochondria, and chloroplasts. Class II chaperonins, or TCP1 proteins include both the thermosomes or TF55 proteins of Archaea and the CCT proteins of eukaryotes. The eukaryotic species are composed of two octameric rings, while thermosomes may have either 8 or 9-member rings. Class II chaperonins do not have a helper protein. Class II chaperonins are very closely related to Class I chaperonins by structure, but not by sequence. For more information, see Pieces: GroEL.",,,,,,
III. DnaK from DnaJ and GrpE:
Link:
tinyurl.com/ml9bt2
www-nmr.cabm.rutgers.edu/photogallery/proteins
/htm/page19.htm
....."DnaJ is a heat shock induced protein from the bacterium Escherichia coli which is under control of thr htpr regulatory protein. DnaJ interacts with the chaperone Hsp70-like DnaK protein to disassemble a protein complex found at a phage lambda's origin of replication (ORI). Also, DnaJ with the joint effort of GrpE stimulates the ATPase activity of DnaK. DnaJ, DnaK, and GrpE are all involved in a variety of biological processes: protein folding and transport, cell survival at high temperatures, negative autoregulation of the heat shock response, and the replication of bacteriophage lambda and other plasmids.
DnaJ is 376 amino acid residues long. However, the N-terminal amino acid residues 2-108 retain much of the entire protein's biological function and capabilities. Within this region is the J domain, comprised of residues 2-72. It consists of four alpha helices: 1=Blue, 2=Green, 3=Pink, and 4=Gold. Helices 2 and 3 are in an antiparallel fashion, and in the center of this polypeptide fragment is a conserved hydrophobic core.".......
=================
IV. GrpE
Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J; , Science 1997;276:431-435.: Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. PUBMED:9103205
Interpro entry IPR000740
Molecular chaperones are a diverse family of proteins that function to protect proteins in the intracellular milieu from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-terminal ATP-hydrolysing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. In prokaryotes the grpE protein. Dimeric GrpE is the co-chaperone for DnaK, and acts as a nucleotide exchange factor, stimulating the rate of ADP release 5000-fold PUBMED:8280473.[/u] DnaK is itself a weak ATPase; ATP hydrolysis by DnaK is stimulated by its interaction with another co-chaperone, DnaJ. Thus the co-chaperones DnaJ and GrpE are capable of tightly regulating the nucleotide-bound and substrate-bound state of DnaK in ways that are necessary for the normal housekeeping functions and stress-related functions of the DnaK molecular chaperone cycle.
The X-ray crystal structure of GrpE in complex with the ATPase domain of DnaK revealed that GrpE is an asymmetric homodimer, bent in a manner that favours extensive contacts with only one DnaKATPase monomer PUBMED:15136046. GrpE does not actively compete for the atomic positions occupied by the nucleotide. GrpE and ADP mutually reduce one another's affinity for DnaK 200-fold, and ATP instantly dissociates GrpE from DnaK."
V. Sigma 32: it is an rpoH gene product.
links:
www.wikigenes.org/e/gene/e/947970.html
tinyurl.com/l6h3mp
www.ihop-net.org/UniPub/iHOP/gs/171051.html?
list=1&page=1
Note the different proteins affiliated with.
Here is what the Sigma H reacts to and notice all in e-coli,
this was the first organism they used as a model, now if it is
a model, might they just be using it to incorporate the dimers
(artificial) proteins into us. If there is problems with the polypeptide
then herein is the first use of this catianic artificial polymer into
live peptides.?.......
VI. Dimeric GrpE
VII. Llamda Bacteriophage
www.pubmedcentral.nih.gov/articlerender.fcgi?artid=390449
Finally found Janelle Farms again........will check them out. affiliated
with HHMI How Hughs Med Institute. and others......They could
be trying to fix this or carry on as usual. Incidentally heat shock
proteins are supposed to be what they call "immortal genes", but,
in my mind they are artificial peptides, proteins, being integrated
in. Do you ever notice that the fibers do not seem real, like they
have an artificial non degrading, non dissolving (insoluable) factor
to them? In otherwords, they can't be burned, do not dissolve,
only when dry or out of the medium, our mucus, our plasma, our
blood, etc. once out of the source they fall apart. Seems prions
are like that as well, seems prions have something to do with
the unfolding and folding as well.
So, DnaK is a CHAPERONIN homologenous to HSP 70(heat shock protein 70) of eukaryotes (mulicelled) ??KDNA?
Works with DnaJ (e-coli), and GrpE (from prokaryote(directed
constructed evolution,) ADP-dependent, folding of polypeptide.
They fused the prokaryote to the eukaryote in this novel
creation.
DnaK is a heat shock protein.
when not in heat shock mode degrades alpha 32? .."an RNA polymerase regulator which detects the promoter sites for transcription of RNA coding for heat shock proteins"
sigma 32 is a rpoH,
GrpE and Dimeric GrpE
DIMERS ARE MAN MADE..................
okay the Lamda phage is what we need to look at and
start with
DnaA.......THE INITIATION Protein O and protein P
next post.
skyship