Actin homolog MreB and RNA polymerase interact and are both required for chromosome segregation in Escherichia coli

被引:103
作者
Kruse, T
Blagoev, B
Lobner-Olesen, A
Wachi, M
Sasaki, K
Iwai, N
Mann, M
Gerdes, K [1 ]
机构
[1] Univ So Denmark, Dept Biochem & Mol Biol, DK-5230 Odense M, Denmark
[2] Roskilde Univ Ctr, Dept Chem & Life Sci, DK-4000 Roskilde, Denmark
[3] Max Planck Inst Biochem, D-82152 Martinsried, Germany
[4] Tokyo Inst Technol, Dept Bioengn, Yokohama, Kanagawa 227, Japan
关键词
MreB; actin; RNA polymerase (RNAP); chromosome segregation; oriC; terC;
D O I
10.1101/gad.366606
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The actin-like MreB cytoskeletal protein and RNA polymerase (RNAP) have both been suggested to provide the force for chromosome segregation. Here, we identify MreB and RNAP as in vivo interaction partners. The interaction was confirmed using in vitro purified components. We also present convincing evidence that MreB and RNAP are both required for chromosome segregation in Escherichia coli. MreB is required for origin and bulk DNA segregation, whereas RNAP is required for bulk DNA, terminus, and possibly also for origin segregation. Furthermore, flow cytometric analyses show that MreB depletion and inactivation of RNAP confer virtually identical and highly unusual chromosome segregation defects. Thus, our results raise the possibility that the MreB-RNAP interaction is functionally important for chromosome segregation.
引用
收藏
页码:113 / 124
页数:12
相关论文
共 73 条
[1]  
Bellomy G R, 1990, Prog Nucleic Acid Res Mol Biol, V39, P81, DOI 10.1016/S0079-6603(08)60624-8
[2]   Defining a centromere-like element in Bacillus subtilis by identifying the binding sites for the chromosome-anchoring protein RacA [J].
Ben-Yehuda, S ;
Fujita, M ;
Liu, XS ;
Gorbatyuk, B ;
Skoko, D ;
Yan, J ;
Marko, JF ;
Liu, JS ;
Eichenberger, P ;
Rudner, DZ ;
Losick, R .
MOLECULAR CELL, 2005, 17 (06) :773-782
[3]   RacA, a bacterial protein that anchors chromosomes to the cell poles [J].
Ben-Yehuda, S ;
Rudner, DZ ;
Losick, R .
SCIENCE, 2003, 299 (5606) :532-536
[4]   Opinion - Actin up in the nucleus [J].
Bettinger, BT ;
Gilbert, DM ;
Amberg, DC .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2004, 5 (05) :410-415
[5]   Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics [J].
Blagoev, B ;
Ong, SE ;
Kratchmarova, I ;
Mann, M .
NATURE BIOTECHNOLOGY, 2004, 22 (09) :1139-1145
[6]   A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling [J].
Blagoev, B ;
Kratchmarova, I ;
Ong, SE ;
Nielsen, M ;
Foster, LJ ;
Mann, M .
NATURE BIOTECHNOLOGY, 2003, 21 (03) :315-318
[7]   TIMING OF CHROMOSOMAL REPLICATION IN ESCHERICHIA-COLI [J].
BOYE, E ;
LOBNEROLESEN, A ;
SKARSTAD, K .
BIOCHIMICA ET BIOPHYSICA ACTA, 1988, 951 (2-3) :359-364
[8]   The dynamic nuclear redistribution of an hnRNP K-homologous protein during Drosophila embryo development and heat shock. Flexibility of transcription sites in vivo [J].
Buchenau, P ;
Saumweber, H ;
ArndtJovin, DJ .
JOURNAL OF CELL BIOLOGY, 1997, 137 (02) :291-303
[9]   Interaction network containing conserved and essential protein complexes in Escherichia coli [J].
Butland, G ;
Peregrín-Alvarez, JM ;
Li, J ;
Yang, WH ;
Yang, XC ;
Canadien, V ;
Starostine, A ;
Richards, D ;
Beattie, B ;
Krogan, N ;
Davey, M ;
Parkinson, J ;
Greenblatt, J ;
Emili, A .
NATURE, 2005, 433 (7025) :531-537
[10]   The distribution of RNA polymerase in Escherichia coli is dynamic and sensitive to environmental cues [J].
Cabrera, JE ;
Jin, DJ .
MOLECULAR MICROBIOLOGY, 2003, 50 (05) :1493-1505