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Putative cobalt- and nickel-binding proteins and motifs in Streptococcus pneumoniae - PubMed

Putative cobalt- and nickel-binding proteins and motifs in Streptococcus pneumoniae

Xuesong Sun et al. Metallomics. 2013 Jun.

Abstract

Cobalt and nickel play important roles in various biological processes. The present work focuses on the enrichment and identification of Co- and Ni-binding motifs and proteins in Gram-positive bacteria. Immobilized metal affinity column (IMAC) was used to partially enrich putative metal-binding proteins and peptides from Streptococcus pneumoniae, and then LTQ-Orbitrap mass spectrometry (MS) was applied to identify and characterize the metal-binding motifs and proteins. In total, 208 and 223 proteins were isolated by Co- and Ni-IMAC columns respectively, in which 129 proteins were present in both preparations. Based on the gene ontology (GO) analysis, the putative metal-binding proteins were found to be mainly involved in protein metabolism, gene expression regulation and carbohydrate metabolism. These putative metal-binding proteins form a highly connected network, indicating that they may synergistically work together to achieve specific biological functions. Putative Co- and Ni-binding motifs were identified with H(X)nH, M(X)nH and H(X)nM derived from the identified 51 Co-binding peptides and 66 Ni-binding peptides. Statistics of frequency of amino acids in the metal-binding motifs showed that cobalt and nickel prefer to bind histidine and methionine, but not cysteine. These results obtained by a systematic metalloproteomic approach provide important clues for the further investigation of metal homeostasis and metal-related virulence of bacteria.

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Putative cobalt- and nickel-binding proteins and motifs in Streptococcus pneumoniae - PubMed