Potential Involvement of N-Terminal Acetylation in the Quantitative Regulation of the ε Subunit of Chloroplast ATP Synthase under Drought Stress

Bioscience, Biotechnology and Biochemistry

Volumn 77, Issue 5, 2013, Pages 998-1007

  Hoshiyasu, Saki ^a   Kohzuma, Kaori ^a   Yoshida, Kazuo ^a   Fujiwara, Masayuki ^a   Fukao, Yoichiro ^a   Akiho Yokota, ^a   Akashi, Kinya ^a,b  

^a NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^b TOTTORI UNIVERSITY   (Japan)

Author keywords

Acetylation; ATP synthase subunit; Chloroplast; Drought; Metalloaminopeptidase

Indexed keywords

ATP SYNTHASE; CHLOROPLAST; CITRULLUS LANATUS; ISO-ELECTRIC POINTS; METALLO-PROTEASE; METALLOAMINOPEPTIDASE; PROTEOME ANALYSIS; STRUCTURAL DIFFERENCES;

ACETYLATION; ENERGY CONVERSION; MASS SPECTROMETRY;

DROUGHT;

ADENOSINE TRIPHOSPHATE; AMINOPEPTIDASE; ISOENZYME; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ACETYLATION; AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; CHEMISTRY; CITRULLUS; DROUGHT; ENZYMOLOGY; HYDROLYSIS; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGICAL STRESS; PHYSIOLOGY; PROTEIN SUBUNIT;

ACETYLATION; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; AMINOPEPTIDASES; CHLOROPLAST PROTON-TRANSLOCATING ATPASES; CITRULLUS; DROUGHTS; HYDROLYSIS; ISOENZYMES; MOLECULAR SEQUENCE DATA; PROTEIN SUBUNITS; STRESS, PHYSIOLOGICAL;

CITRULLUS LANATUS; CITRULLUS LANATUS VAR. LANATUS;

EID: 84878701862     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.120945     Document Type: Article

References (48)

1. Field CB, Behrenfeld MJ, Randerson JT, and Falkowski P, Science, 281, 237-240 (1998).
2. Li Z, Wakao S, Fischer BB, and Niyogi KK, Annu. Rev. Plant, 60, 239-260 (2009).
3. Walters RG, J. Exp. Bot., 56, 435-447 (2005).
4. Walters RG and Horton P, Planta, 195, 248-256 (1994).
5. Shimizu M, Kato H, Ogawa T, Kurachi A, Nakagawa Y, and Kobayashi H, Proc. Natl. Acad. Sci. USA, 107, 10760-10764 (2010).
6. Yang D-H, Webster J, Adam Z, Lindahl M, and Andersson B, Plant Physiol., 118, 827-834 (1998).
7. Vener AV, Biochim. Biophys. Acta, 1767, 449-457 (2007).
8. Aro E-M, Suorsa M, Rokka A, Allahverdiyeva Y, Paakkarinen V, Saleem A, Battchikova N, and Rintamaki E, J. Exp. Bot., 56, 347-356 (2005).
9. Raunser S, Magnani R, Huang Z, Houtz RL, Trievel RC, Penczek PA, and Walz T, Proc. Natl. Acad. Sci. USA, 106, 3160-3165 (2009).
10. Nanjo Y, Oka H, Ikarashi N, Kaneko K, Kitajima A, Mitsui T, Munoz FJ, Rodriguez-Lopez M, Baroja-Femandez E, and Pozueta-Romero J, Plant Cell, 18, 2582-2592 (2006).
11. Houtz RL, Stults JT, Mulligan RM, and Tolbert NE, Proc. Natl. Acad. Sci. USA, 86, 1855-1859 (1989).
12. Zybailov B, Rutschow H, Friso G, Rudella A, Emanuelsson O, Sun Q, and van Wijk KJ, PLoS ONE, 23, e1994 (2008).
13. Allen JF, Cell, 110, 273-276 (2002).
14. Kramer DM, Cruz JA, and Kanazawa A, Trends Plant Sci., 8, 27-32 (2003).
15. Rott M, Martins NF, Thiele W, Lein W, Bock R, Kramer DM, and Schottler MA, Plant Cell, 23, 304-321 (2011).
16. Yamori W, Takahashi S, Makino A, Price GD, Badger MR, and von Caemmerer S, Plant Physiol., 155, 956-962 (2011).
17. Kohzuma K, Cruz JA, Akashi K, Hoshiyasu S, Munekage YN, Yokota A, and Kramer DM, Plant Cell Environ., 32, 209-219 (2009).
18. Akashi K, Yoshimura K, Nanasato Y, Takahara K, Munekage Y, and Yokota A, Plant Biotechnol., 25, 257-263 (2008).
19. Sanda S, Yoshida K, Kuwano M, Kawamura T, Munekage YN, Akashi K, and Yokota A, Physiol. Plant., 142, 247-264 (2011).
20. Evron Y, Johnson EA, and McCarty RE, J. Bioenerg. Biomembr., 32, 501-506 (2000).
21. Johnson E and Melis A, Photosynth. Res., 82, 131-140 (2004).
22. Akashi K, Yoshida K, Kuwano M, Kajikawa M, Yoshimura K, Hoshiyasu S, Inagaki N, and Yokota A, Planta, 233, 947-960 (2011).
23. Ogawa T, Nishimura K, Aoki T, Takase H, Tomizawa K, Ashida H, and Yokota A, Plant Physiol., 151, 114-128 (2009).
24. Kim JS, Jung JD, Lee JA, Park HW, Oh KH, Jeong WJ, Choi DW, Liu JR, and Cho KY, Plant Cell Rep., 25, 334-340 (2006).
25. Binder A, Jagendorf A, and Ngo E, J. Biol. Chem., 253, 3094-3100 (1978).
26. Akashi K, Nishimura N, Ishida Y, and Yokota A, Biochem. Biophys. Res. Commun., 323, 72-78 (2004).
27. Fujiwara M, Umemura K, Kawasaki T, and Shimamoto K, Plant Physiol., 140, 734-745 (2006).
28. Hisabori T, Kothen G, and Strotmann H, J. Biochem., 114, 324-328 (1993).
29. Bernkop-Schnürch A and Marschütz MK, Pharm. Res., 14, 181-185 (1997).
30. Shinozaki K, Deno H, Kato A, and Sugiura M, Gene, 24, 47-155 (1983).
31. Plader W, Yukawa Y, Sugiura M, and Malepszy S, Cell. Mol. Biol. Lett., 12, 584-594 (2007).
32. Giglione C and Meinnel T, Trends Plant Sci., 6, 566-572 (2001).
33. Mann M and Jensen ON, Nat. Biotechnol., 21, 255-261 (2003).
34. Walling LL, Curr. Opin. Plant Biol., 9, 227-233 (2006).
35. Driessen HPC, Ramaekers FCS, Vree Egberts WTM, Dodemont HJ, de Jong WW, Tesser GI, and Bloemendal H, Eur. J. Biochem., 136, 403-406 (1983).
36. Jayawardene DS and Dass C, Peptides, 20, 963-970 (1999).
37. Polevoda B and Sherman F, J. Biol. Chem., 275, 36479-36482 (2000).
38. Falb M, Aivaliotis M, Garcia-Rizo C, Bisle B, Tebbe A, Klein C, Konstantinidis K, Siedler F, Pfeiffer F, and Oesterhelt D, J. Mol. Biol., 362, 915-924 (2006).
39. Persson B, Flinta C, von Heijne G, and Jörnvall H, Eur. J. Biochem., 152, 523-527 (1985).
40. Kim G-W and Yang X-J, Trends Biochem. Sci., 36, 211-220 (2011).
41. Jornvall H, J. Theor. Biol., 55, 1-12 (1975).
42. Mischerikow N and Heck AJR, Proteomics, 11, 571-589 (2011).
43. Brown JL, J. Biol. Chem., 254, 1447-1449 (1979).
44. Michel H, Hunt DF, Shabanowitz J, and Bennett J, J. Biol. Chem., 263, 1123-1130 (1988).
45. Polevoda B and Sherman F, J. Mol. Biol., 325, 595-622 (2003).
46. Soppa J, Archaea, 16, pii:820681 (2010).
47. Pesaresi P, Gardner NA, Masiero S, Dietzmann A, Eichacker L, Wickner R, Salamini F, and Leister D, Plant Cell, 15, 1817-1832 (2003).
48. Yokthongwattana C, Mahong B, Roytrakul S, Phaonaklop N, Narangajavana J, and Yokthongwattana K, Planta, 235, 649-659 (2012).