title: Strain-resolved community proteomics reveals recombining genomes of acidophilic bacteria.
abstract: Microbes comprise the majority of extant organisms, yet much remains to be learned about the nature and driving forces of microbial diversification. Our understanding of how microorganisms adapt and evolve can be advanced by genome-wide documentation of the patterns of genetic exchange, particularly if analyses target coexisting members of natural communities. Here we use community genomic data sets to identify, with strain specificity, expressed proteins from the dominant member of a genomically uncharacterized, natural, acidophilic biofilm. Proteomics results reveal a genome shaped by recombination involving chromosomal regions of tens to hundreds of kilobases long that are derived from two closely related bacterial populations. Inter-population genetic exchange was confirmed by multilocus sequence typing of isolates and of uncultivated natural consortia. The findings suggest that exchange of large blocks of gene variants is crucial for the adaptation to specific ecological niches within the very acidic, metal-rich environment. Mass-spectrometry-based discrimination of expressed protein products that differ by as little as a single amino acid enables us to distinguish the behaviour of closely related coexisting organisms. This is important, given that microorganisms grouped together as a single species may have quite distinct roles in natural systems and their interactions might be key to ecosystem optimization. Because proteomic data simultaneously convey information about genome type and activity, strain-resolved community proteomics is an important complement to cultivation-independent genomic (metagenomic) analysis of microorganisms in the natural environment.
authors.affiliation: University of California, Berkeley, California 94720, USA.
authors.forename: Ian
authors.initials: I
authors.lastname: Lo
authors.forename: Vincent J
authors.initials: VJ
authors.lastname: Denef
authors.forename: Nathan C
authors.initials: NC
authors.lastname: Verberkmoes
authors.forename: Manesh B
authors.initials: MB
authors.lastname: Shah
authors.forename: Daniela
authors.initials: D
authors.lastname: Goltsman
authors.forename: Genevieve
authors.initials: G
authors.lastname: DiBartolo
authors.forename: Gene W
authors.initials: GW
authors.lastname: Tyson
authors.forename: Eric E
authors.initials: EE
authors.lastname: Allen
authors.forename: Rachna J
authors.initials: RJ
authors.lastname: Ram
authors.forename: J Chris
authors.initials: JC
authors.lastname: Detter
authors.forename: Paul
authors.initials: P
authors.lastname: Richardson
authors.forename: Michael P
authors.initials: MP
authors.lastname: Thelen
authors.forename: Robert L
authors.initials: RL
authors.lastname: Hettich
authors.forename: Jillian F
authors.initials: JF
authors.lastname: Banfield
mesh_terms: D000595:Amino Acid Sequence; D001419:Bacteria / Q000737:chemistry / Q000145:classification* / Q000201:enzymology / Q000235:genetics*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics*; D018441:Biofilms / Q000145:classification; D016680:Genome, Bacterial / Q000235:genetics*; D023281:Genomics; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000235:genetics; D020543:Proteome / Q000737:chemistry / Q000235:genetics; D040901:Proteomics; D011995:Recombination, Genetic / Q000235:genetics*; D012273:Ribulose-Bisphosphate Carboxylase / Q000737:chemistry / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D010455:Peptides; D020543:Proteome; D012273:Ribulose-Bisphosphate Carboxylase