The human ATP synthase β subunit gene: Sequence analysis, chromosome assignment, and differential expression

Neckelmann, Nicolas; Warner, Cynthia K.; Chung, Andrew B.; Kudoh, Jun; Minoshima, Shinsei; Fukuyama, Ryuichi; Maekawa, Masahiko; Shimizu, Yoshiko; Shimizu, Nobuyoshi; Liu, Jean D.; Wallace, Douglas C.

doi:10.1016/0888-7543(89)90125-0

Cited by 67 publications

(28 citation statements)

References 48 publications

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“…The observed profiles in different tissues were again very similar to those of mRNAs of COX subunits indicating that the levels of nuclear transcripts of ATPase and COX subunits are in close relation (the ATPase fl-subunit mRNA/COX VIb mRNA arbitrary ratio was 1.26 in liver, 0.85 in BAT, I in heart, 1.1 in muscle and 0.87 in brain) and that the expression of nuclear and mitochondrial genes investigated is well coordinated in tissues that differ 2.4-13.8-fold (BAT vs. other tissues) in transcriptional activity (Table II). The results are in agreement with the differential expression of the ATPase fi-subunit gene in human tissues [18] and FEBS LETTERS December 1991 l~nsilometric data of fl-subunit and COX Vlh mRNAs were expreascd in % of heart values. Relativ~ levels of transcripts were calculated per mg wet weight and in relation to the content of ATPas¢ and COX, respectively.…”

Section: Resultssupporting

confidence: 84%

“…As shown in Table I, both the COX activity and COX content, measured immunochemic:~lly as the content of the COX IV subunit, were found to be highest in BAT, when compared with heart, liver, muscle and brain. Oligomycin-sensitive ATPase activity cannot be precisely measured in tissue homogenates" therefore, the enzyme was quantified as the content of the highly homologous ATPasc ~-subunit [6,18] using anti-F~ antibodies, in line with previous reports [2,3] the content of ATPase was lowest in BAT, both absolutely and in relation to the COX content. The respective ATPase/COX ratio was thus 5-11-times lower in BAT.…”

Section: Resultsmentioning

confidence: 80%

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Low content of mitochondrial ATPase in brown adipose tissue is the result of post‐transcriptional regulation

et al. 1991

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The mI~NA levels of ATPase/5, ATPase 6, cytochrome oxidase (COX) Vlb and COX I subunit~ were found to be 2.4~13.8-fold higher in brown adipose tissue (BAT) than in heart, skeletal muscle, brain and liver of mice. The comparison with tissue contents of ATPase and COX revealed that the sele~=tive, 5-1 l-fold reduction of ATPase in BAT is not caused by decreased transcription of ATPase genes. Likewise, the ATPase ]~ and COX Vlb mRNA levels in cultured brown adipocytes were also not influenced by norepinephrine, which activated the expression of the UCP gene by two orders of magnitude. The results indicate that the biosynthesis of mitochondrial ATPase in BAT is post-transcriptionally regulatm~l. lional events are responsible for the selective reduction of the ATPase content in BAT. MATERIALS AND METHODSFour-week-old mice of Balb/c outbred strain were maintained at room temperature, on a 12 h light/12 h dark cycle. When indicated, animals were exposed to 4°C prior to use. The animals were killed by decapitation and ti.ssue samples for RNA isolation were frozen in liquid nitrogen. For other assays, 5~ homog~.:ates [w/v) were prepared in 0.25 M sucrose, 10 mM Tris/HCI, I mM EDTA, pH 7.4, and filtered through a 250/Jm nylon screen.The stromal-vascular ceils from BAT were isolated and cultivated as previously [71. Experiments were performed with cells cultured for 7 days.Total RNA was isolated as described in [8] and checked for purity and integrity. For Northern blot analysis, 20Mg RNA aliqnots were denatured in the presence of glyoxaL separated by eleetrophoresis in 1.2% agaros¢ gel and transferred to a nylon membrane (Hybond-N, Amersham) according to standard procedures [9]. Hybridization was carried out overnight at 68°C in 5x Dcnhardt's solution, 5x SSC, 50 mM sodium phosphate, pH 6.5. 0. !% SDS and 250 pg/ml of herring sperm DNA. Blots were washed in 2× SSC, 0.1 ~b SDS (2x |5 min, room temp.) and 0.Ix SSC, 0.1% SDS (2× 15 rain, 55°C). Following autoradiography the blots were stripped for 60 rain at 95~C in 0. I SDS and sequentially re-hybridized with several DNA pr3bes.The eDNA probes were generously provided by the following investigators: 1.26 kb E.coR! fragment of the rat ATPase /~-subunR eDNA in pUCI9

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Section: Resultssupporting

confidence: 84%

Section: Resultsmentioning

confidence: 80%

Low content of mitochondrial ATPase in brown adipose tissue is the result of post‐transcriptional regulation

et al. 1991

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“…OXBOX element acts as a positive regulatory element exclusively in muscle cells (Li et al, 1990). Therefore, the OXBOX and its associated trans-activating factor(s) might account for the high ANTl expression in heart and skeletal muscle in association with F 0 F 1 -ATP synthase b subunit, a component of the oxidative phosphorylation machinery (Li et al, 1989;Neckelmann et al, 1989). The relatively ANT isoforms family C Brenner et al low level of mitochondrial transcripts in skeletal muscle is inconsistent with the high level of ANTl and F 0 F 1 -ATP synthase b subunit transcripts.…”

Section: Ant1 Isoform Is Pro-apoptotic and Its Expression Is Frequentmentioning

confidence: 99%

Adenine nucleotide translocase family: four isoforms for apoptosis modulation in cancer

et al. 2010

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“…It is also less expressed in liver and kidney. These findings suggest that tissue-specific mRNA levels of ATP5B can occur with transcriptional control (Neckelmann et al, 1989). The exact function of ATP5B is not known and the level of ATP5B gene expression has been shown to fall in different human tumors as compared to normal tissues (Willers et al, 2010).…”

Section: Transcriptionmentioning

confidence: 99%

“…ATP5B gene consists of four "CCAAT" sequences upstream and these sequences are much closer to the transcriptional initiation site (Neckelmann et al, 1989). This gene encodes a single transcript as presented in NCBI database.…”

mentioning

confidence: 99%

ATP5B (ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide)

Bozgeyik¹,

Arman²,

İğci³

2017

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Review on ATP5B, with data on DNA/RNA, on the protein encoded and where the gene is implicated. IdentityOther names: ATPMB, ATPSB, HEL-S-271 HGNC (Hugo): ATP5B Location: 12q13.3 DNA/RNA DescriptionThe human ATP5B gene is located on the minus strand and spans 7894 bps of genomic region (56638175 -56646068). ATP5B gene sequence shows partial homology with chromosomes 2 and 17. There are 13 Alu repeat sequences. Among these sequences, 4 were found to be inside the intron and the rest were towards the upstream side.

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The human ATP synthase β subunit gene: Sequence analysis, chromosome assignment, and differential expression

Cited by 67 publications

References 48 publications

Low content of mitochondrial ATPase in brown adipose tissue is the result of post‐transcriptional regulation

Low content of mitochondrial ATPase in brown adipose tissue is the result of post‐transcriptional regulation

Adenine nucleotide translocase family: four isoforms for apoptosis modulation in cancer

ATP5B (ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide)

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