A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO

被引：144

作者：

Ashida, H

Saito, Y

Kojima, C

Kobayashi, K

Ogasawara, N

Yokota, A

机构：

[1] Nara Inst Sci & Technol, Grad Sch Biol Sci, Nara 6300101, Japan

[2] Res Inst Innovat Technol Earth, Plant Mol Physiol Lab, Kyoto 6190292, Japan

来源：

SCIENCE | 2003年 / 302卷 / 5643期

关键词：

D O I：

10.1126/science.1086997

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The genomes of several nonphotosynthetic bacteria, such as Bacillus subtilis, and some Archaea include genes for proteins with sequence homology to the large subunit of ribulose bisphosphate carboxylase/oxygenase (RuBisCO). We found that such a RuBisCO-like protein (RLP) from B. subtilis catalyzed the 2,3-diketo-5-methylthiopentyl-1-phosphate enolase reaction in the methionine salvage pathway. A growth-defective mutant, in which the gene for this RLP had been disrupted, was rescued by the gene for RuBisCO from the photosynthetic bacterium Rhodospirillum rubrum. Thus, the photosynthetic RuBisCO from R. rubrum retains the ability to function in the methionine salvage pathway in B. subtilis.

引用

页码：286 / 290

页数：5

共 29 条

[1]

Andrews T.J., 1987, BIOCH PLANTS, P131, DOI 10.1016/B978-0-12-675410-0.50009-9

[2]

ASHIDA H, UNPUB

[3]

Avigad G, 1975, Methods Enzymol, V41, P27

[4] A SIGNATURE OF THE OXYGENASE INTERMEDIATE IN CATALYSIS BY RIBULOSE-BISPHOSPHATE CARBOXYLASE OXYGENASE AS PROVIDED BY A SITE-DIRECTED MUTANT [J].

CHEN, YR ;

HARTMANN, FC .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (20) :11741-11744

[5] Mechanism of Rubisco: The carbamate as general base [J].

Cleland, WW ;

Andrews, TJ ;

Gutteridge, S ;

Hartman, FC ;

Lorimer, GH .

CHEMICAL REVIEWS, 1998, 98 (02) :549-561

[6] Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae [J].

Dai, Y ;

Pochapsky, TC ;

Abeles, RH .

BIOCHEMISTRY, 2001, 40 (21) :6379-6387

[7] The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium [J].

Eisen, JA ;

Nelson, KE ;

Paulsen, IT ;

Heidelberg, JF ;

Wu, M ;

Dodson, RJ ;

Deboy, R ;

Gwinn, ML ;

Nelson, WC ;

Haft, DH ;

Hickey, EK ;

Peterson, JD ;

Durkin, AS ;

Kolonay, JL ;

Yang, F ;

Holt, I ;

Umayam, LA ;

Mason, T ;

Brenner, M ;

Shea, TP ;

Parksey, D ;

Nierman, WC ;

Feldblyum, TV ;

Hansen, CL ;

Craven, MB ;

Radune, D ;

Vamathevan, J ;

Khouri, H ;

White, O ;

Gruber, TM ;

Ketchum, KA ;

Venter, JC ;

Tettelin, H ;

Bryant, DA ;

Fraser, CM .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (14) :9509-9514

[8] MOST ABUNDANT PROTEIN IN THE WORLD [J].

ELLIS, RJ .

TRENDS IN BIOCHEMICAL SCIENCES, 1979, 4 (11) :241-244

[9] Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1 [J].

Ezaki, S ;

Maeda, N ;

Kishimoto, T ;

Atomi, H ;

Imanaka, T .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (08) :5078-5082

[10]

FURFINE ES, 1988, J BIOL CHEM, V263, P9598

← 1 2 3 →