Identification and characterization of a cDNA encoding a long-chain cis-isoprenyltranferase involved in dolichyl monophosphate biosynthesis in the ER of brain cells

Shridas, Preetha; Rush, Jeffrey S.; Waechter, Charles J.

doi:10.1016/j.bbrc.2003.11.065

Cited by 39 publications

(28 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Activity of the enzyme was 25 and 33% higher in the membranes from ULJK09/ 04 and ULJK21/04, respectively, than in the control. The level of the activity was comparable with the one observed in animal cells (Ericsson et al, 1992;Grunler et al, 1995;Shridas et al, 2003) and signiWcantly lower than in yeast (Sato et al, 1999). The increase in enzyme activity in vitro was lower than that expected from the huge amount of the RER2 transcript.…”

Section: Expression Of S Cerevisiae Rer2 Gene In T Reeseisupporting

confidence: 83%

Overexpression of the Saccharomyces cerevisiae RER2 gene in Trichoderma reesei affects dolichol dependent enzymes and protein glycosylation

Perlińska-Lenart¹,

Bańkowska²,

Palamarczyk³

et al. 2006

Fungal Genetics and Biology

View full text Add to dashboard Cite

Section: Expression Of S Cerevisiae Rer2 Gene In T Reeseisupporting

confidence: 83%

Overexpression of the Saccharomyces cerevisiae RER2 gene in Trichoderma reesei affects dolichol dependent enzymes and protein glycosylation

Perlińska-Lenart¹,

Bańkowska²,

Palamarczyk³

et al. 2006

Fungal Genetics and Biology

View full text Add to dashboard Cite

“…By contrast, AT2G23410, which catalyzes the formation of dolichol with a chain length of C 120 , was able to complement the rer2 mutant phenotype (Cunillera et al, 2000;Oh et al, 2000). Similarly, a cDNA that encodes a cis-prenyltransferase for catalyzing the production of dolichols with a chain length of C 85 to C 95 from human brain complemented the growth and other phenotypes of the rer2 mutant (Shridas et al, 2003). Studies on the rer2 mutant overexpressing SRT1 indicated that yeast cells are able to utilize the longer dolichols in protein glycosylation when shorter ones (C 70 to C 85 ) are lacking (Sato et al, 2001).…”

Section: Discussionmentioning

confidence: 98%

Dolichol Biosynthesis and Its Effects on the Unfolded Protein Response and Abiotic Stress Resistance in Arabidopsis

Ohyama²,

et al. 2008

View full text Add to dashboard Cite

Dolichols are long-chain unsaturated polyisoprenoids with multiple cellular functions, such as serving as lipid carriers of sugars used for protein glycosylation, which affects protein trafficking in the endoplasmic reticulum. The biological functions of dolichols in plants are largely unknown. We isolated an Arabidopsis thaliana mutant, lew1 (for leaf wilting1), that showed a leaf-wilting phenotype under normal growth conditions. LEW1 encoded a cis-prenyltransferase, which when expressed in Escherichia coli catalyzed the formation of dolichol with a chain length around C 80 in an in vitro assay. The lew1 mutation reduced the total plant content of main dolichols by ;85% and caused protein glycosylation defects. The mutation also impaired plasma membrane integrity, causing electrolyte leakage, lower turgor, reduced stomatal conductance, and increased drought resistance. Interestingly, drought stress in the lew1 mutant induced higher expression of the unfolded protein response pathway genes BINDING PROTEIN and BASIC DOMAIN/LEUCINE ZIPPER60 as well as earlier expression of the stress-responsive genes RD29A and COR47. The lew1 mutant was more sensitive to dark treatment, but this dark sensitivity was suppressed by drought treatment. Our data suggest that LEW1 catalyzes dolichol biosynthesis and that dolichol is important for plant responses to endoplasmic reticulum stress, drought, and dark-induced senescence in Arabidopsis.

show abstract

“…Therefore, Rv1086 may not be a good drug target in M. tuberculosis as speculated earlier [89], even though synthesis of Dec-P appears to be essential. In addition, enthusiasm for Rv2361c and Rv1086 as potential drug targets is tempered by the observation that these enzymes have 35 and 33% identity (respectively) with the enzyme identified as the polyprenyl diphosphate synthase involved in dolichyl phosphate synthesis in human brain [102]. However, as noted above, IPP is a precursor of Pol-P, and, in fact, is a precursor of all of the tens of thousands of extraordinarily chemically and structurally diverse known isoprenoid compounds found through out nature [103].…”

Section: The Central Role Of Polyprenyl Phos-phate In Cell-wall Synthmentioning

confidence: 98%

The Cell-Wall Core of Mycobacterium tuberculosis in the Context of Drug Discovery.

Brennan¹,

Crick²

2007

CTMC

116

121

View full text Add to dashboard Cite

Present-day understanding of the architecture of the entire cell-wall of Mycobacterium tuberculosis amounts to a "core" template comprised of peptidoglycan with phosphodiester linkage, via a linker disaccharide, to a linear D-galactofuran, to which, in turn, are attached several strands of a highly branched D-arabinofuran. The cell-wall mycolic acids are linked via an ester to the majority of the non-reducing termini of the D-arabinan. The mycolic acids are oriented perpendicular to the plane of the membrane and provide a truly special lipid barrier responsible for many of the physiological and disease-inducing aspects of M. tuberculosis. Intercalated within this environment are the phthiocerol dimycocerosates, cord factor or dimycolyltrehalose, sulfolipids, phosphatidylinositol mannosides and the related lipomannan and lipoarabinomannan, etc., agents responsible for much of the pathogenesis of tuberculosis. Interest in the biosynthesis of the cell-wall core, regarded, unlike the ancillary lipids, as essential to bacterial viability and integrity, is now driven by the pressing need for alternative drugs to counteract drug-resistant tuberculosis. In a manner analogous to the roles of lipid I and II in peptidglycan formation, synthesis of the entire arabinogalactan is initiated by transferring activated sugars to decaprenyl-phosphate, giving rise to the linker disaccharide, followed by stepwise elongation of the galactan, and the arabinan, apparently one sugar at a time. The genetics and enzymology of these polymerization events have not been well defined, nor have the final steps, namely the attachment of mycolic acids and ligation to peptidoglycan. However, what is known of the earlier events in cell-wall core synthesis has attracted interest in terms of new anti-tuberculosis drug development.

show abstract

Identification and characterization of a cDNA encoding a long-chain cis-isoprenyltranferase involved in dolichyl monophosphate biosynthesis in the ER of brain cells

Cited by 39 publications

References 37 publications

Overexpression of the Saccharomyces cerevisiae RER2 gene in Trichoderma reesei affects dolichol dependent enzymes and protein glycosylation

Overexpression of the Saccharomyces cerevisiae RER2 gene in Trichoderma reesei affects dolichol dependent enzymes and protein glycosylation

Dolichol Biosynthesis and Its Effects on the Unfolded Protein Response and Abiotic Stress Resistance in Arabidopsis

The Cell-Wall Core of Mycobacterium tuberculosis in the Context of Drug Discovery.

Contact Info

Product

Resources

About