Inactivation of Ribosomal Protein Genes in Bacillus subtilis Reveals Importance of Each Ribosomal Protein for Cell Proliferation and Cell Differentiation

被引:81
作者
Akanuma, Genki [3 ]
Nanamiya, Hideaki [1 ,2 ]
Natori, Yousuke [1 ,2 ]
Yano, Koichi [1 ,2 ]
Suzuki, Shota [1 ,2 ]
Omata, Shuya [3 ]
Ishizuka, Morio [3 ]
Sekine, Yasuhiko [1 ,2 ]
Kawamura, Fujio [1 ,2 ]
机构
[1] Rikkyo Univ, Coll Sci, Dept Life Sci, Toshima Ku, Tokyo 171, Japan
[2] Rikkyo Univ, Coll Sci, Res Ctr Life Sci, Toshima Ku, Tokyo 171, Japan
[3] Chuo Univ, Fac Sci & Engn, Dept Appl Chem, Bunkyo Ku, Tokyo 112, Japan
关键词
ESCHERICHIA-COLI; TRANSFER-RNA; ANGSTROM RESOLUTION; MESSENGER-RNA; THIOSTREPTON-RESISTANT; STRUCTURAL BASIS; MUTANTS; SUBUNIT; SPORULATION; L11;
D O I
10.1128/JB.01544-12
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Among the 57 genes that encode ribosomal proteins in the genome of Bacillus subtilis, a Gram-positive bacterium, 50 genes were targeted by systematic inactivation. Individual deletion mutants of 16 ribosomal proteins (L1, L9, L15, L22, L23, L28, L29, L32, L33.1, L33.2, L34, L35, L36, S6, S20, and S21) were obtained successfully. In conjunction with previous reports, 22 ribosomal proteins have been shown to be nonessential in B. subtilis, at least for cell proliferation. Although several mutants that harbored a deletion of a ribosomal protein gene did not show any significant differences in any of the phenotypes that were tested, various mutants showed a reduced growth rate and reduced levels of 70S ribosomes compared with the wild type. In addition, severe defects in the sporulation frequency of the Delta rplA (L1) mutant and the motility of the Delta rpsU (S21) mutant were observed. These data provide the first evidence in B. subtilis that L1 and S21 are required for the progression of cellular differentiation.
引用
收藏
页码:6282 / 6291
页数:10
相关论文
共 65 条
  • [51] STOFFLER G, 1984, J BIOL CHEM, V259, P4521
  • [52] A MUTANT FROM ESCHERICHIA-COLI WHICH LACKS RIBOSOMAL PROTEIN-S17 AND PROTEIN-L29 USED TO LOCALIZE THESE 2 PROTEINS ON THE RIBOSOMAL SURFACE
    STOFFLERMEILICKE, M
    DABBS, ER
    ALBRECHTEHRLICH, R
    STOFFLER, G
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1985, 150 (03): : 485 - 490
  • [53] Quantitative Proteomic Analysis of Ribosome Assembly and Turnover In Vivo
    Sykes, Michael T.
    Shajani, Zahra
    Sperling, Edit
    Beck, Andrea H.
    Williamson, James R.
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2010, 403 (03) : 331 - 345
  • [54] MRNA helicase activity of the ribosome
    Takyar, S
    Hickerson, RP
    Noller, HF
    [J]. CELL, 2005, 120 (01) : 49 - 58
  • [55] EFFECTS ON GROWTH AND SPORULATION OF INACTIVATION OF A BACILLUS-SUBTILIS GENE (CTC) TRANSCRIBED INVITRO BY MINOR VEGETATIVE CELL RNA-POLYMERASES (E-SIGMA-37, E-SIGMA-32)
    TRUITT, CL
    WEAVER, EA
    HALDENWANG, WG
    [J]. MOLECULAR & GENERAL GENETICS, 1988, 212 (01): : 166 - 171
  • [56] Limitation of ribosomal protein L11 availability in vivo affects translation termination
    Van Dyke, N
    Xu, WB
    Murgola, EJ
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2002, 319 (02) : 329 - 339
  • [58] WALLECZEK J, 1989, J BIOL CHEM, V264, P4231
  • [59] WIENEN B, 1979, J BIOL CHEM, V254, P8031
  • [60] Structure of the 30S ribosomal subunit
    Wimberly B.T.
    Brodersen D.E.
    Clemons Jr. W.M.
    Morgan-Warren R.J.
    Carter A.P.
    Vonrheln C.
    Hartsch T.
    Ramakrishnan V.
    [J]. Nature, 2000, 407 (6802) : 327 - 339