title: Structural rearrangement in an RsmA/CsrA ortholog of Pseudomonas aeruginosa creates a dimeric RNA-binding protein, RsmN.
abstract: In bacteria, the highly conserved RsmA/CsrA family of RNA-binding proteins functions as global posttranscriptional regulators acting on mRNA translation and stability. Through phenotypic complementation of an rsmA mutant in Pseudomonas aeruginosa, we discovered a family member, termed RsmN. Elucidation of the RsmN crystal structure and that of the complex with a hairpin from the sRNA, RsmZ, reveals a uniquely inserted α helix, which redirects the polypeptide chain to form a distinctly different protein fold to the domain-swapped dimeric structure of RsmA homologs. The overall β sheet structure required for RNA recognition is, however, preserved with compensatory sequence and structure differences, allowing the RsmN dimer to target binding motifs in both structured hairpin loops and flexible disordered RNAs. Phylogenetic analysis indicates that, although RsmN appears unique to P. aeruginosa, homologous proteins with the inserted α helix are more widespread and arose as a consequence of a gene duplication event.
authors: School of Chemistry, Centre for Biomolecular Sciences, University of Nottingham, Nottingham NG7 2RD, UK.
authors: Elizabeth R
authors: ER
authors: Morris
authors: Gareth
authors: G
authors: Hall
authors: Chan
authors: C
authors: Li
authors: Stephan
authors: S
authors: Heeb
authors: Rahul V
authors: RV
authors: Kulkarni
authors: Laura
authors: L
authors: Lovelock
authors: Hazel
authors: H
authors: Silistre
authors: Marco
authors: M
authors: Messina
authors: Miguel
authors: M
authors: Cámara
authors: Jonas
authors: J
authors: Emsley
authors: Paul
authors: P
authors: Williams
authors: Mark S
authors: MS
authors: Searle
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001483:Base Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D055029:Inverted Repeat Sequences; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011550:Pseudomonas aeruginosa; D012329:RNA, Bacterial / Q000737:chemistry; D016601:RNA-Binding Proteins / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D012329:RNA, Bacterial; D016601:RNA-Binding Proteins
references: Mol Microbiol. 2005 Feb;55(3):724-38
references: 15660999
references: FEMS Microbiol Rev. 2011 Mar;35(2):247-74
references: 20738404
references: J Biomed Sci. 2001 Mar-Apr;8(2):160-9
references: 11287746
references: Mol Microbiol. 2003 May;48(3):657-70
references: 12694612
references: Proc Natl Acad Sci U S A. 2005 Nov 22;102(47):17136-41
references: 16286659
references: Mol Microbiol. 2003 Nov;50(4):1361-79
references: 14622422
references: Appl Environ Microbiol. 2010 Feb;76(3):910-21
references: 20023108
references: Res Microbiol. 2005 Jan-Feb;156(1):7-16
references: 15636743
references: J Mol Biol. 1992 Aug 20;226(4):943-57
references: 1325563
references: J Bacteriol. 1997 Jul;179(14):4639-42
references: 9226279
references: RNA Biol. 2013 Jun;10(6):1031-41
references: 23635605
references: Proteins. 2005 Nov 1;61(2):449-53
references: 16104018
references: J Med Microbiol. 2003 Jan;52(Pt 1):19-28
references: 12488561
references: Mol Microbiol. 2004 Jan;51(1):15-32
references: 14651608
references: J Bacteriol. 1993 Aug;175(15):4744-55
references: 8393005
references: Trends Biochem Sci. 1998 Sep;23(9):358-61
references: 9787643
references: Mol Microbiol. 2009 May;72(3):612-32
references: 19426209
references: J Bacteriol. 2001 Mar;183(6):1870-80
references: 11222584
references: J Mol Biol. 2009 Sep 18;392(2):511-28
references: 19619561
references: J Mol Biol. 2006 Feb 3;355(5):1026-36
references: 16359708
references: J Bacteriol. 1996 Feb;178(4):1012-7
references: 8576033
references: J Bacteriol. 2001 Nov;183(22):6676-83
references: 11673439
references: Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21
references: 20057044
references: J Bacteriol. 2005 May;187(10):3496-501
references: 15866937
references: J Bacteriol. 1995 Sep;177(17):5108-15
references: 7665490
references: J Bacteriol. 2005 Jan;187(1):276-85
references: 15601712
references: Nucleic Acids Res. 2014 Jun;42(11):6811-25
references: 24782516
references: Biochem Biophys Res Commun. 2007 Jan 19;352(3):769-73
references: 17141182
references: Mol Microbiol. 1998 Jul;29(1):219-34
references: 9701816
references: J Bacteriol. 2004 May;186(10):2936-45
references: 15126453
references: Appl Environ Microbiol. 1995 May;61(5):1959-67
references: 7646031
references: Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):14073-8
references: 10570200
references: RNA. 2005 Oct;11(10):1579-87
references: 16131593
references: Mol Microbiol. 2001 Apr;40(1):245-56
references: 11298291
references: Phytopathology. 1998 Jul;88(7):678-84
references: 18944940
references: Nature. 2000 Aug 31;406(6799):959-64
references: 10984043
references: Environ Microbiol. 2013 Feb;15(2):313-24
references: 22672726
references: PLoS Pathog. 2013;9(7):e1003508
references: 23935486
references: Nat Struct Mol Biol. 2007 Sep;14(9):807-13
references: 17704818
references: RNA Biol. 2012 Apr;9(4):379-91
references: 22336760
references: Mol Microbiol. 2002 Jun;44(6):1599-610
references: 12067347
references: J Bacteriol. 2002 Feb;184(4):1046-56
references: 11807065
references: Mol Microbiol. 2011 May;80(4):868-85
references: 21375594
references: Cell Mol Life Sci. 2010 Sep;67(17):2897-908
references: 20446015