Transiently Transfected Purine Biosynthetic Enzymes Form Stress Bodies

Zhao, Alice; Tsechansky, Mark; Swaminathan, Jagannath; Cook, Lindsey; Ellington, Andrew D.; Marcotte, Edward M.
February 2013
PLoS ONE;Feb2013, Vol. 8 Issue 2, p1
Academic Journal
It has been hypothesized that components of enzymatic pathways might organize into intracellular assemblies to improve their catalytic efficiency or lead to coordinate regulation. Accordingly, de novo purine biosynthesis enzymes may form a purinosome in the absence of purines, and a punctate intracellular body has been identified as the purinosome. We investigated the mechanism by which human de novo purine biosynthetic enzymes might be organized into purinosomes, especially under differing cellular conditions. Irregardless of the activity of bodies formed by endogenous enzymes, we demonstrate that intracellular bodies formed by transiently transfected, fluorescently tagged human purine biosynthesis proteins are best explained as protein aggregation.


Related Articles

  • Difference in the distribution pattern of substrate enzymes in the metabolic network of Escherichia coli, according to chaperonin requirement. Takemoto, Kazuhiro; Niwa, Tatsuya; Taguchi, Hideki // BMC Systems Biology;2011, Vol. 5 Issue 1, p98 

    Background: Chaperonins are important in living systems because they play a role in the folding of proteins. Earlier comprehensive analyses identified substrate proteins for which folding requires the chaperonin GroEL/GroES (GroE) in Escherichia coli, and they revealed that many chaperonin...

  • Optimal Kinetics for Chaperonin Assisted Protein Folding. Goncharenko, Igor; Gopinathan, Ajay // AIP Conference Proceedings;5/8/2009, Vol. 1127 Issue 1, p13 

    The problem of optimizing the yield rate in reactions that are catalyzed by enzymes is of fundamental importance. In the case of protein folding catalyzed by chaperonins, there is a distinct possibility of the formation of misfolded proteins within the chaperonin nano-cage which can be...

  • Interaction specificity between the chaperone and proteolytic components of the cyanobacterial Clp protease. TRYGGVESSON, Anders; STÅHLBERG, Frida M.; MOGK, Axel; ZETH, Kornelius; CLARKE, Adrian K. // Biochemical Journal;9/ 1/2012, Vol. 446 Issue 2, p311 

    The Clp protease is conserved among eubacteria and most eukaryotes, and uses ATP to drive protein substrate unfolding and translocation into a chamber of sequestered proteolytic active sites. In plant chloroplasts and cyanobacteria, the essential constitutive Clp protease consists of the...

  • A molecular chaperone inducer protects neurons from ER stress. Kudo, T.; Kanemoto, S.; Hara, H.; Morimoto, N.; Morihara, T.; Kimura, R.; Tabira, T.; Imaizumi, K.; Takeda, M. // Cell Death & Differentiation;Feb2008, Vol. 15 Issue 2, p364 

    The endoplasmic reticulum (ER) stress response is a defense system for dealing with the accumulation of unfolded proteins in the ER lumen. Recent reports have shown that ER stress is involved in the pathology of some neurodegenerative diseases and cerebral ischemia. In a screen for compounds...

  • Mutant SOD1 detoxification mechanisms in intact single cells. Ganesan, S.; Rohde, G.; Eckermann, K.; Sroka, K.; Schaefer, M. K. E.; Dohm, C. P.; Kermer, P.; Haase, G.; Wouters, F.; Bähr, M.; Weishaupt, J. H. // Cell Death & Differentiation;Feb2008, Vol. 15 Issue 2, p312 

    Mutant superoxide dismutase 1 (mtSOD1) causes dominantly inherited amyotrophic lateral sclerosis (ALS). The mechanism for mtSOD1 toxicity remains unknown. Two main hypotheses are the impairment of proteasomal function and chaperone depletion by misfolded mtSOD1. Here, we employed FRET/FLIM and...

  • Antibodies as specific chaperones. Ermolenko, D.N.; Zherdev, A.V.; Dzantiev, B.B. // Biochemistry (00062979);Nov2004, Vol. 69 Issue 11, p1233 

    Protein folding is often accompanied by formation of non-native conformations leading to protein aggregation. A number of reports indicate that antibodies can facilitate folding and prevent aggregation of protein antigens. The influence of antibodies on folding is strictly antigen specific....

  • Protein Folding, Misfolding, and Aggregation. Formation of Inclusion Bodies and Aggresomes. Markossian, K. A.; Kurganov, B. I. // Biochemistry (00062979);Sep2004, Vol. 69 Issue 9, p971 

    In this review the mechanisms of protein folding, misfolding, and aggregation as well as the mechanisms of cell defense against toxic protein aggregates are considered. Misfolded and aggregated proteins in cells are exposed to chaperonemediated refolding and are degraded by proteasomes if...

  • Tubulin folding: the special case of a beta-tubulin isotype from the Antarctic psychrophilic ciliate Euplotes focardii. Pucciarelli, Sandra; Chiappori, Federica; Sparvoli, Daniela; Milanesi, Luciano; Miceli, Cristina; Melki, Ronald // Polar Biology;Dec2013, Vol. 36 Issue 12, p1833 

    Folding assistance is a fundamental requirement of certain proteins, and it may be subjected to physicochemical constraints in case of organisms adapted to polar temperatures. Limited information is available about protein folding in the polar environment. Folding of tubulin provides one of the...

  • Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Rye, Hays S.; Burston, Steven G. // Nature;8/21/1997, Vol. 388 Issue 6644, p792 

    Presents research which shows that for the protein folding of malate dehydrogenase and Rubisco there is an absolute requirement for ATP in the cis ring. Role of chaperonin GroEL in efficient folding of proteins; Binding and hydrolysis of ATP; Why GroEL functions as a double-ring complex.


Read the Article


Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics