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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제29권 제8호
- 발행연도
- 2019.1
- 수록면
- 1,288 - 1,298 (11page)
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초록· 키워드
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Bacterial ATP synthases drive ATP synthesis by a rotary mechanism, and play a vital role in physiology and cell metabolism. Corynebacterium glutamicum is well known as an industrial workhorse for amino acid production, and its ATP synthase operon contains eight structural genes and two adjacent genes, cg1360 and cg1361. So far, the physiological functions of Cg1360 (GenBank CAF19908) and Cg1361 (GenBank CAF19909) remain unclear. Here, we showed that Cg1360 was a hydrophobic protein with four transmembrane helices (TMHs), while no TMH was found in Cg1361. Deletion of cg1360, but not cg1361, led to significantly reduced cell growth using glucose and acetic acid as carbon sources, reduced F1 portions in the membrane, reduced ATP-driven proton-pumping activity and ATPase activity, suggesting that Cg1360 plays an important role in ATP synthase function. The intracellular ATP concentration in the Δcg1360 mutant was decreased to 72% of the wild type, while the NADH and NADPH levels in the Δcg1360 mutant were increased by 29% and 26%, respectively. However, the Δcg1361 mutant exhibited comparable intracellular ATP, NADH and NADPH levels with the wild-type strain. Moreover, the effect of cg1360 deletion on L-valine production was examined in the L-valine-producing V-10 strain. The final production of L-valine in the V-10-Δcg1360 mutant reached 9.2 ± 0.3 g/l in shake flasks, which was 14% higher than that of the V-10 strain. Thus, Cg1360 can be used as an effective engineering target by altering energy metabolism for the enhancement of amino acid production in C. glutamicum.
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참고문헌 (46)
참고문헌 신청
Nakamoto RK / 2008 / The rotary mechanism of the ATP synthase / Arch. Biochem. Biophys 476:43~50
von Ballmoos C / 2009 / Essentials for ATP synthesis by F1Fo-ATP synthases / Annu. Rev. Biochem 78:649~672
Hicks DB / 2010 / F1Fo-ATP synthases of alkaliphilic bacteria : lessons from their adaptations / Biochim. Biophys. Acta 1797:1362~1377
Kulish O / 2016 / F1 rotary motor of ATP synthase is driven by the torsionally-asymmetric drive shaft / Sci. Rep 6:28180
Nesci S / 2015 / Opposite rotation directions in the synthesis and hydrolysis of ATP by the ATP synthase : hints from a subunit asymmetry / J. Membr. Biol 248:163~169
von Ballmoos C / 2009 / Essentials for ATP synthesis by F1Fo-ATP synthases / Annu. Rev. Biochem 78:649~672
Hicks DB / 2010 / F1Fo-ATP synthases of alkaliphilic bacteria : lessons from their adaptations / Biochim. Biophys. Acta 1797:1362~1377
Kulish O / 2016 / F1 rotary motor of ATP synthase is driven by the torsionally-asymmetric drive shaft / Sci. Rep 6:28180
Nesci S / 2015 / Opposite rotation directions in the synthesis and hydrolysis of ATP by the ATP synthase : hints from a subunit asymmetry / J. Membr. Biol 248:163~169
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