Difference between revisions of "RplL"

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(Extended information on the protein)
(Expression and regulation)
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=Expression and regulation=
 
=Expression and regulation=
  
* '''Operon:'''  
+
* '''Operon:''' ''[[rplJ]]-[[rplL]]'' {{PubMed|26101249}}
  
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rplL_120607_120978_1 rplL] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rplL_120607_120978_1 rplL] {{PubMed|22383849}}
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* '''Regulation:'''  
 
* '''Regulation:'''  
 
** [[RelA]] dependent downregulation (Class I) during stringent response {{PubMed|11948165}}
 
** [[RelA]] dependent downregulation (Class I) during stringent response {{PubMed|11948165}}
 +
** termination/ antitermination ([[rplJ|L10]]-[[rplL|L12]]<sub>4</sub> complex) {{PubMed|26101249}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 +
** [[rplJ|L10]]-[[rplL|L12]]<sub>4</sub> complex: transcription termination (attenuation) at excess of the complex (autorepression) {{PubMed|26101249}}
  
 
* '''Additional information:'''
 
* '''Additional information:'''

Revision as of 09:25, 23 July 2015

Gene name rplL
Synonyms
Essential yes PubMed
Product ribosomal protein L12 (BL9)
Function translation
Gene expression levels in SubtiExpress: rplL
Interactions involving this protein in SubtInteract: RplL
MW, pI 12 kDa, 4.355
Gene length, protein length 369 bp, 123 aa
Immediate neighbours rplJ, ybxB
Sequences Protein DNA DNA_with_flanks
Genetic context
RplL context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RplL expression.png















Categories containing this gene/protein

translation, essential genes, membrane proteins, most abundant proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU01050

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
    • termination/ antitermination (L10-L124 complex) PubMed
  • Regulatory mechanism:
    • L10-L124 complex: transcription termination (attenuation) at excess of the complex (autorepression) PubMed
  • Additional information:
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 24809 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 142727 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 20697 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 11499 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 19060 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Helen Yakhnin, Alexander V Yakhnin, Paul Babitzke
Ribosomal protein L10(L12)4 autoregulates expression of the Bacillus subtilis rplJL operon by a transcription attenuation mechanism.
Nucleic Acids Res: 2015, 43(14);7032-43
[PubMed:26101249] [WorldCat.org] [DOI] (I p)

Yun Chen, Shu Feng, Veerendra Kumar, Rya Ero, Yong-Gui Gao
Structure of EF-G-ribosome complex in a pretranslocation state.
Nat Struct Mol Biol: 2013, 20(9);1077-84
[PubMed:23912278] [WorldCat.org] [DOI] (I p)

Genki Akanuma, Hideaki Nanamiya, Yousuke Natori, Koichi Yano, Shota Suzuki, Shuya Omata, Morio Ishizuka, Yasuhiko Sekine, Fujio Kawamura
Inactivation of ribosomal protein genes in Bacillus subtilis reveals importance of each ribosomal protein for cell proliferation and cell differentiation.
J Bacteriol: 2012, 194(22);6282-91
[PubMed:23002217] [WorldCat.org] [DOI] (I p)

Matthew A Lauber, William E Running, James P Reilly
B. subtilis ribosomal proteins: structural homology and post-translational modifications.
J Proteome Res: 2009, 8(9);4193-206
[PubMed:19653700] [WorldCat.org] [DOI] (P p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

James R Iben, David E Draper
Specific interactions of the L10(L12)4 ribosomal protein complex with mRNA, rRNA, and L11.
Biochemistry: 2008, 47(9);2721-31
[PubMed:18247578] [WorldCat.org] [DOI] (P p)

Catherine Wicker-Planquart, Anne-Emmanuelle Foucher, Mathilde Louwagie, Robert A Britton, Jean-Michel Jault
Interactions of an essential Bacillus subtilis GTPase, YsxC, with ribosomes.
J Bacteriol: 2008, 190(2);681-90
[PubMed:17981968] [WorldCat.org] [DOI] (I p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)

K J Boor, M L Duncan, C W Price
Genetic and transcriptional organization of the region encoding the beta subunit of Bacillus subtilis RNA polymerase.
J Biol Chem: 1995, 270(35);20329-36
[PubMed:7657605] [WorldCat.org] [DOI] (P p)