Solution structure of a BolA‐like protein from Mus musculus

The BolA‐like proteins are widely conserved from prokaryotes to eukaryotes. The BolA‐like proteins seem to be involved in cell proliferation or cell‐cycle regulation, but the molecular function is still unknown. Here we determined the structure of a mouse BolA‐like protein. The overall topology is αββααβα, in which β1 and β2 are antiparallel, and β3 is parallel to β2. This fold is similar to the class II KH fold, except for the absence of the GXXG loop, which is well conserved in the KH fold. The conserved residues in the BolA‐like proteins are assembled on the one side of the protein.

[1]  M. de Pedro,et al.  The gene bolA regulates dacA (PBP5), dacC (PBP6) and ampC (AmpC), promoting normal morphology in Escherichia coli , 2002, Molecular microbiology.

[2]  M. Aldea,et al.  Division genes in Escherichia coli are expressed coordinately to cell septum requirements by gearbox promoters. , 1990, The EMBO journal.

[3]  S. Grzesiek,et al.  NMRPipe: A multidimensional spectral processing system based on UNIX pipes , 1995, Journal of biomolecular NMR.

[4]  K. Sharp,et al.  Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons , 1991, Proteins.

[5]  Ana C. Messias,et al.  Structural Basis for Recognition of the Intron Branch Site RNA by Splicing Factor 1 , 2001, Science.

[6]  Yasuhiko Yoshida,et al.  Cell‐free production and stable‐isotope labeling of milligram quantities of proteins , 1999, FEBS letters.

[7]  S. Park,et al.  Regulation of septation and cytokinesis during resumption of cell division requires uvi31+, a UV-inducible gene of fission yeast. , 2002, Molecules and cells.

[8]  M Aldea,et al.  Identification, cloning, and expression of bolA, an ftsZ-dependent morphogene of Escherichia coli , 1988, Journal of bacteriology.

[9]  M. Billeter,et al.  MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.

[10]  C. Vonrhein,et al.  Structure of the 30S ribosomal subunit , 2000, Nature.

[11]  R. Hengge-aronis,et al.  Growth phase-regulated expression of bolA and morphology of stationary-phase Escherichia coli cells are controlled by the novel sigma factor sigma S , 1991, Journal of bacteriology.

[12]  G. Clore,et al.  Structure and dynamics of KH domains from FBP bound to single-stranded DNA , 2002, Nature.

[13]  G. Clore,et al.  Molecular basis of sequence‐specific single‐stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single‐stranded DNA , 2002, The EMBO journal.

[14]  D. Court,et al.  Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[15]  N. Grishin,et al.  KH domain: one motif, two folds. , 2001, Nucleic acids research.

[16]  J. Thornton,et al.  AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR , 1996, Journal of biomolecular NMR.

[17]  R. Darnell,et al.  Sequence-Specific RNA Binding by a Nova KH Domain Implications for Paraneoplastic Disease and the Fragile X Syndrome , 2000, Cell.

[18]  Bruce A. Johnson,et al.  NMR View: A computer program for the visualization and analysis of NMR data , 1994, Journal of biomolecular NMR.

[19]  J. Thompson,et al.  The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. , 1997, Nucleic acids research.

[20]  C. Arraiano,et al.  The stationary‐phase morphogene bolA from Escherichia coli is induced by stress during early stages of growth , 1999, Molecular microbiology.

[21]  J. K. Lee,et al.  Isolation of UV-inducible transcripts from Schizosaccharomyces pombe. , 1994, Biochemical and biophysical research communications.

[22]  M. Aldea,et al.  Induction of a growth‐phase‐dependent promoter triggers transcription of bolA, an Escherichia coli morphogene. , 1989, The EMBO journal.

[23]  R J Read,et al.  Crystallography & NMR system: A new software suite for macromolecular structure determination. , 1998, Acta crystallographica. Section D, Biological crystallography.

[24]  C. Bult,et al.  Functional annotation of a full-length mouse cDNA collection , 2001, Nature.

[25]  Torsten Herrmann,et al.  Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. , 2002, Journal of molecular biology.

[26]  R. Seong,et al.  Identification and expression of uvi31+, a UV‐inducible gene from Schizosaccharomyces pombe , 1997, Environmental and molecular mutagenesis.

[27]  E. Birney,et al.  Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs , 2002, Nature.

[28]  C. Sander,et al.  Protein structure comparison by alignment of distance matrices. , 1993, Journal of molecular biology.

[29]  A. Bax,et al.  Protein backbone angle restraints from searching a database for chemical shift and sequence homology , 1999, Journal of biomolecular NMR.