Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme

Russell, George C.; Guest, John R.

doi:10.1016/0167-4838(91)90271-z

Cited by 59 publications

(45 citation statements)

References 31 publications

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“…The catalytic domain of PDC-E2 is apparent in the Xenopus cDNA sequence (Fig. 5A) and contains the conserved CoA binding site (Russell and Guest, 1991). As also expected, the Xenopus PDC-E2 sequence (Fig.…”

Section: Vp67 Is a Xenopus Homolog Of Pdc-e2mentioning

confidence: 60%

“…The Xenopus PDC-E2 cDNA sequence contains all domains characteristic of dihydrolipoamide acetyltransferase (Bleile et al, 1981;Packman et al, 1984;De Marcucci et al, 1988;Thekkumkara et al, 1988;Russell and Guest, 1991;Matuda et al, 1992), including a mitochondrial targeting signal, two lipoyl-binding domains, a conserved E1/E3 subunit binding domain, and a CoA binding site within the conserved C-terminal catalytic domain (Fig. 5A).…”

Section: Vp67 Is a Xenopus Homolog Of Pdc-e2mentioning

confidence: 99%

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Apparent mitochondrial asymmetry in Xenopus eggs

Володина

Denegre

Mowry

2003

Developmental Dynamics

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Section: Vp67 Is a Xenopus Homolog Of Pdc-e2mentioning

confidence: 60%

Section: Vp67 Is a Xenopus Homolog Of Pdc-e2mentioning

confidence: 99%

Apparent mitochondrial asymmetry in Xenopus eggs

Володина

Denegre

Mowry

2003

Developmental Dynamics

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“…This occurs despite the significant degree of sequence identity seen between PDC components from different mammalian species. Sequence comparison between PDC of human and rat origin (data are not yet available for murine and bovine PDC) show 90% identity for PDC-E2 (Russell and Guest, 1991) and 99% and 97% for the available sequences of the E1␣ and E1␤ components (Matuda et al, 1992). In contrast to the fully cross-reactive B-cell responses, over the time course of the current study (8 weeks), the splenic T-cell response induced by sensitization with bovine PDC was restricted to epitopes specific for the non-self-bovine protein, because no proliferative or cytokine response was observed after in vitro stimulation with self-PDC.…”

Section: Discussionmentioning

confidence: 99%

Investigation of a Mechanism for Accelerated Breakdown of Immune Tolerance to the Primary Biliary Cirrhosis–Associated Autoantigen, Pyruvate Dehydrogenase Complex

Jones

Palmer

Bennett

et al. 2002

Laboratory Investigation

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SUMMARY: Primary biliary cirrhosis (PBC) is an autoimmune liver disease characterized by autoreactive T-and B-cell responsesto the highly conserved enzyme pyruvate dehydrogenase complex (PDC). In this study we have examined the breakdown of T-cell tolerance to self-PDC using a mouse model. Female SJL/J mice were sensitized intraperitoneally with foreign-PDC (bovine) and/or self-PDC (murine) in complete Freund's adjuvant, and serum, spleen, and liver tissue was taken 8 weeks later. Animals sensitized with foreign-PDC produced IgG antibodies that were reactive with both foreign and self-PDC, but splenic T cells from these animals only responded to stimulation with foreign PDC. Sensitization with self-PDC elicited neither antibodies nor reactive T cells. Significantly, cosensitization with mixed self-PDC and foreign-PDC resulted in a full breakdown of self-tolerance, with generation of both antibody and T-cell responses to self-PDC of the type seen exclusively in human PBC patients. Mild bile duct lesions deficient in CD8 ϩ T cells were seen 8 weeks after sensitization with either foreign or self-PDC. However, after sensitization with mixed self-PDC and foreign-PDC, these lesions were significantly larger and heavily infiltrated by CD8 ϩ T cells. Liver-infiltrating T cells derived from the self-PDC and foreign-PDC cosensitized but not from control animals showed reactivity with self-PDC, suggesting a possible role for autoreactive PDC-specific T-cell responses in the pathogenesis of the observed histologic changes. It is likely that B-cell cross-reactivity between foreign and self-PDC enhances the potential for breakdown of T-cell self-tolerance by allowing efficient presentation of self-antigens in the inoculum. This model may provide a useful system for investigating the etiology and treatment of PBC. (Lab Invest 2002, 82:211-219).

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“…1b). These residues were predicted from comparison of a number of E2 sequences with that of chloramphenicol acetyltransferase (41) and were confirmed by site-directed substitutions of E2p. For the E. coli PDHc with H602C E2p substitution, no overall PDHc activity or E2p acetyltransferase activity were detected, and with the S550A substitution, the PDHc activity was drastically reduced; however, the ability to bind the E1p and E3 components and the reductive acetylation of the lipoyl domain by E1p were not affected (42,43).…”

Section: Overall Description Of the E2pcd X-ray Structure-threementioning

confidence: 99%

Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex

Wang

Nemeria

Chandrasekhar

et al. 2014

Journal of Biological Chemistry

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Background: The E. coli pyruvate dehydrogenase complex catalyzes conversion of pyruvate to acetyl-CoA and comprises E1p, E2p, and E3 components. Results: The structure of the E2 core domain was solved and shown to efficiently catalyze acetyl transfer between domains. Conclusion: Mass spectrometry revealed hitherto unrecognized domain-induced interactions between E1 and E2 core domain. Significance: A multifaceted approach is required to understand communication between intact multidomain components.

show abstract

Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme

Cited by 59 publications

References 31 publications

Apparent mitochondrial asymmetry in Xenopus eggs

Apparent mitochondrial asymmetry in Xenopus eggs

Investigation of a Mechanism for Accelerated Breakdown of Immune Tolerance to the Primary Biliary Cirrhosis–Associated Autoantigen, Pyruvate Dehydrogenase Complex

Structure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase Complex

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