Dataset Information

Streptococcus pneumoniae metal homeostasis alters cellular metabolism

ABSTRACT: Streptococcus pneumoniae parental T4R and Δ1434-8 strains were cultured in quadruplicated in C+Y medium. Proteins were isolated, quantified, trypsin digested, and analyzed by 1D LC ESI MS/MS.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Streptococcus Pneumoniae Tigr4

SUBMITTER: Justin Thornton

LAB HEAD: Justin Thornton

PROVIDER: PXD019773 | Pride | 2020-07-22

REPOSITORIES: Pride

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<i>Streptococcus pneumoniae</i> metal homeostasis alters cellular metabolism.

Burcham Lindsey R LR Hill Rebecca A RA Caulkins Rachel C RC Emerson Joseph P JP Nanduri Bindu B Rosch Jason W JW Fitzkee Nicholas C NC Thornton Justin A JA

Metallomics : integrated biometal science 20200901 9

Streptococcus pneumoniae colonizes the human nasopharyngeal mucosa and is a leading cause of community-acquired pneumonia, acute otitis media, and bacterial meningitis. Metal ion homeostasis is vital to the survival of this pathogen across diverse biological sites and contributes significantly to colonization and invasive disease. Microarray and qRT-PCR analysis revealed an upregulation of an uncharacterized operon (SP1433-1438) in pneumococci subjected to metal-chelation by N,N,N',N'-tetrakis-( ...[more]

PMID: 32676626

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Project description:A novel ArsR-SmtB family transcriptional repressor, KmtR, has been characterised from mycobacteria. Mutants of M. tuberculosis lacking kmtR show elevated expression of Rv2025c encoding a deduced CDF-family metal-exporter. KmtR-dependent repression of the cdf and kmtR operator-promoters was alleviated by nickel and cobalt in minimal medium. Electrophoretic mobility shift assays (EMSA) and fluorescence anisotropy (FA) show binding of purified KmtR to nucleotide sequences containing a region of dyad symmetry from the cdf and kmtR operator-promoters. A relatively large deltar(obs) in FA implies formation of high order apo-KmtR(n)-DNA and multiple complexes were detected by EMSA. Incubation of KmtR with cobalt inhibits DNA-complex assembly and metal-protein binding was confirmed by competition against 4-(2-pyridylazo)-resorcinol. KmtR is the second, to NmtR, characterised ArsR-SmtB sensor of nickel and cobalt from M. tuberculosis suggesting special significance for these ions in this pathogen. KmtR-dependent expression is elevated in complete medium with no increase in response to metals, while NmtR retains a response to nickel and cobalt under these conditions. Mixing equimolar apo-KmtR and apo-NmtR with 0.8 equivalents of nickel or cobalt gave nickel- and cobalt-dependent difference emission spectra similar to nickel(0.8)-KmtR and cobalt(0.8)-KmtR, respectively. Thus, KmtR has tighter affinities for nickel and cobalt than NmtR consistent with basal levels of these metals being sensed by KmtR but not NmtR in complete medium. More than a thousand genes encoding ArsR-SmtB related proteins are listed in databases and a proportion can be predicted to detect metals through known allosteric sites. KmtR has none of the previously defined sites. Substitution of His(88), Glu(101), His(102), His(110) or His(111) with Gln generated KmtR-variants that repress the cdf and kmtR operator-promoters even in elevated nickel and cobalt, revealing a new sensory site. Importantly, ArsR-SmtB sequence groupings do not correspond with the different sensory-motifs revealing that only the latter should be used to predict metal-sensing. Data is also available from http://bugs.sgul.ac.uk/E-BUGS-49

			Action	DRS
	AS_217601.sf3	Other
	AS_217601_DOP_1_QE1.raw	Raw
	AS_217601_DOP_2_QE1.raw	Raw
	AS_217601_DOP_3_QE1.raw	Raw
	AS_217601_DOP_4_QE1.raw	Raw