Gene structure of the human mitochondrial adenosine triphosphate synthase beta subunit.

Ohta, Shigeo; Tomura, Hideaki; Matsuda, Kakuko; Kagawa, Yasuo

doi:10.1016/s0021-9258(18)37950-x

Cited by 83 publications

(6 citation statements)

References 32 publications

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“…The 3 subunit that contains the ATP-binding domain (catalytic site) of the enzyme is a protein encoded by a nuclear gene. In normal ceils it is synthesized in the cytoplasm and translocated to the inner membrane of mitochondria where it associates as a nontransmembrane protein with other subunits of the F1 complex (21,(34)(35)(36). Whereas altered expression of such a molecule on tumor cells was unexpected, previous studies (37)(38)(39)(40) have shown a decrease in ATP synthase activity and a reduction in the content of F1 components in mitochondria isolated from neoplastic cells and from cells of regenerating tissues.…”

Section: Discussionmentioning

confidence: 99%

A novel ligand in lymphocyte-mediated cytotoxicity: expression of the beta subunit of H+ transporting ATP synthase on the surface of tumor cell lines.

Das

Mondragon

Sadeghian

et al. 1994

The Journal of Experimental Medicine

126

109

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SummaryExtracellular adenosine triphosphate (eATP) has been suggested to play a role in lymphocyteinduced tumor destruction. We now provide evidence that a protein responsible for ATP synthesis in mitochondria may also play a physiologic role in major histocompatibility complex-independent, lymphocyte-mediated cytotoxicity. A 51.5-kD protein (p51.5) beating structural and immunologic characteristics of the B subunit of H + transporting ATP synthase (E.C. 3.6.1.34, B-H +ATPase, published molecular mass of 51.6 kD) was detected on the plasma membrane of three different human tumor cell lines studied. NH2-terminal amino acid sequence analysis of purified p51.5 from K562 tumor cells revealed 100% homology of 16 residues identified in the first 21 positions to the known sequence of human mitochondrial B-H § ATPase. Antibody directed against a 2l-iner peptide in the ATP binding region of B-H+ATPase (anti-B) reacted with only one band on Western blots of whole tumor extracts and tumor membrane extracts suggesting that the antiserum reacts with a single species of protein. Anti-B reacted with the cell membranes of tumor ceils as determined by fluorescence-activated flow cytometry and immunoprecipitated a 51.5-kD protein from surface-labeled neoplastic cells (but not human erythrocytes and lymphocytes). Purified p51.5 bound to human lymphocytes and inhibited natural killer (NK) cell-mediated cytotoxicity. Furthermore, anti-B treatment of the K562 and A549 tumor cell lines inhibited NK (by >95%) and interleukin 2-activated killer (LAK) cell (by 75%) cytotoxicity, respectively. Soluble p51.5 upon binding to lymphocytes retained its reactivity to anti-B suggesting that the ATP binding domain and the lymphocyte-receptor binding domain reside in distinct regions of the ligand. These results suggest that B-H +ATPase or a nearly identical molecule is an important ligand in the effector phase (rather than the recognition phase) of a cytolytic pathway used by naive NK and LAK cells.

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Section: Discussionmentioning

confidence: 99%

A novel ligand in lymphocyte-mediated cytotoxicity: expression of the beta subunit of H+ transporting ATP synthase on the surface of tumor cell lines.

Das

Mondragon

Sadeghian

et al. 1994

The Journal of Experimental Medicine

126

109

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“…The transcript that corresponds to one AUG-burdened homeobox cDNA, for example, is restricted to the nucleus (170). Cellular genes that produce mRNAs with upstream AUG codons often use alternative promoters and/or splice sites to generate supplementary transcripts in which the leader sequences are less problematical (68,155,179,197,210,212,223,259,269). Indeed, the 5' variability is sometimes so extensive that no two cDNAs from a given gene have the same 5' noncoding sequence (145,155)!…”

Section: Some Harder Casesmentioning

confidence: 99%

“…7 This is noteworthy because the inhibitory effects of secondary structure may be susceptible to environmental modulation (129) while there is, as yet, no evidence that the inhibitory effects of upstream AUG codons are regulatable in vertebrates, as they are in the GCN4 gene of yeast (86, 220, 267a). In vertebrates, the solution to upstream AUG codons is to get rid of them (68,155,179,197,210,212,223,259,269).…”

Section: Some Harder Casesmentioning

confidence: 99%

The scanning model for translation: an update.

Kozak

1989

The Journal of Cell Biology

3,442

104

2,016

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The small (40S) subunit of eukaryotic ribosomes is believed to bind initially at the capped 5'-end of messenger RNA and then migrate, stopping at the first AUG codon in a favorable context for initiating translation. The first-AUG rule is not absolute, but there are rules for breaking the rule. Some anomalous observations that seemed to contradict the scanning mechanism now appear to be artifacts. A few genuine anomalies remain unexplained.

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“…Single-underlined nucleotides represent an E2F-like sequence within the initiator region that is not protected by E2F1 in the DNase I assay. β-subunit (k40\j206) [18] and mtTFA (k79\j92) [19].…”

Section: Figure 1 the Proximal Region Of Human Cytochrome C 1 Regionmentioning

confidence: 99%

Activity of the human cytochrome c1 promoter is modulated by E2F

Luciaková

Baráth

et al. 2000

Biochem. J.

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The human cytochrome c(1) promoter is strongly activated in transfected Drosophila SL2 cells expressing exogenous human E2F1. Transfection-deletion experiments, DNase I protection by E2F1 and gel mobility-shift experiments locate E2F1 activation sites to two regions on either side of the transcription start site. Deletion of either region prevents E2F1 activation in transfected SL2 cells, suggesting a co-operative interaction between them. E2F6, a member of the E2F family that lacks transactivation domains but contains specific suppressor domains, inhibits cytochrome c(1) promoter activity when co-transfected into HeLa cells, indicating that the E2F proteins modulate the cytochrome c(1) promoter in mammalian cells. However, E2F is not a general regulator of oxidative phosphorylation genes since three additional nuclear-encoded mitochondrial genes were unaffected by E2F1 or E2F6.

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Gene structure of the human mitochondrial adenosine triphosphate synthase beta subunit.

Cited by 83 publications

References 32 publications

A novel ligand in lymphocyte-mediated cytotoxicity: expression of the beta subunit of H+ transporting ATP synthase on the surface of tumor cell lines.

A novel ligand in lymphocyte-mediated cytotoxicity: expression of the beta subunit of H+ transporting ATP synthase on the surface of tumor cell lines.

The scanning model for translation: an update.

Activity of the human cytochrome c1 promoter is modulated by E2F

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