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A molecular key for building hyphae aggregates: the role of the newly identified Streptomyces protein HyaS.

Koebsch I, Overbeck J, Piepmeyer S, Meschke H, Schrempf H - Microb Biotechnol (2009)

Bottom Line: The HyaS protein is dominantly associated with the substrate hyphae.Investigations of ΔH transformants, each carrying a specifically mutated gene, lead to the conclusion that the in situ oxidase activity correlates with the pellet-inducing role of HyaS, and depends on the presence of certain histidine residues.These data present the first molecular basis for future manipulation of pellets, and concomitant production of secondary metabolites during biotechnological processes.

View Article: PubMed Central - PubMed

Affiliation: University of Osnabrück, FB Biology/Chemistry, Applied Genetics of Microorganisms, 49069 Osnabrück, Germany.

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Alignment of HyaS with other hypothetical proteins. Block comparisons of deduced gene products from the streptomycetes S. lividans (S.liv, EMBL, DS: 72304), S. griseus (S.gri, SGR_3840), S. avermitilis (S.ave, SAV_4459), S. scabies (S.sca, 4945557‐4943764), Nocardioides sp. JS614 (N.spe, Noca_1817). The predicted S. coelicolor A3(2) protein (SCO 7657) corresponded to 99% to that of S. lividans; hence, it is not aligned. Amino acid residues, which are identical with the S. lividans protein, are marked white on a black background. The cleavage site, to generate the signal peptide, is indicated by an arrow.
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f1: Alignment of HyaS with other hypothetical proteins. Block comparisons of deduced gene products from the streptomycetes S. lividans (S.liv, EMBL, DS: 72304), S. griseus (S.gri, SGR_3840), S. avermitilis (S.ave, SAV_4459), S. scabies (S.sca, 4945557‐4943764), Nocardioides sp. JS614 (N.spe, Noca_1817). The predicted S. coelicolor A3(2) protein (SCO 7657) corresponded to 99% to that of S. lividans; hence, it is not aligned. Amino acid residues, which are identical with the S. lividans protein, are marked white on a black background. The cleavage site, to generate the signal peptide, is indicated by an arrow.

Mentions: In the course of sequencing larger segments of an unstable genomic DNA region of S. lividans 66 WT (named within the text S. lividans WT) (Betzler et al., 1987), we discovered a reading frame of 1758 bp. This was subsequently (see below) named hyaS (EMBL, DS: 72304). The deduced protein, named HyaS (Fig. 1), comprises 585 amino acids (aa), including a signal peptide. It shares the highest (99%), second highest (73%) and third highest (63%) amino acid identity with, respectively, one hypothetical protein (including a signal peptide) deduced from the Streptomyces coelicolor A3(2) genomic sequence (Bentley et al., 2002), one from the Streptomyces griseus (Ohnishi et al., 2008) and one from the Streptomyces avermitilis genome (Ikeda et al., 2003). Furthermore, a slightly less related deduced protein (586 aa, including the predicted signal peptide) is encoded within the deposited genome of one Streptomyces scabies strain (Fig. 1). DNA–DNA hybridizations and analyses of PCR‐amplified fragments (data not shown) revealed the abundance of hyaS‐related sequences among six additionally tested Streptomyces species (see Experimental procedures).


A molecular key for building hyphae aggregates: the role of the newly identified Streptomyces protein HyaS.

Koebsch I, Overbeck J, Piepmeyer S, Meschke H, Schrempf H - Microb Biotechnol (2009)

Alignment of HyaS with other hypothetical proteins. Block comparisons of deduced gene products from the streptomycetes S. lividans (S.liv, EMBL, DS: 72304), S. griseus (S.gri, SGR_3840), S. avermitilis (S.ave, SAV_4459), S. scabies (S.sca, 4945557‐4943764), Nocardioides sp. JS614 (N.spe, Noca_1817). The predicted S. coelicolor A3(2) protein (SCO 7657) corresponded to 99% to that of S. lividans; hence, it is not aligned. Amino acid residues, which are identical with the S. lividans protein, are marked white on a black background. The cleavage site, to generate the signal peptide, is indicated by an arrow.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3815755&req=5

f1: Alignment of HyaS with other hypothetical proteins. Block comparisons of deduced gene products from the streptomycetes S. lividans (S.liv, EMBL, DS: 72304), S. griseus (S.gri, SGR_3840), S. avermitilis (S.ave, SAV_4459), S. scabies (S.sca, 4945557‐4943764), Nocardioides sp. JS614 (N.spe, Noca_1817). The predicted S. coelicolor A3(2) protein (SCO 7657) corresponded to 99% to that of S. lividans; hence, it is not aligned. Amino acid residues, which are identical with the S. lividans protein, are marked white on a black background. The cleavage site, to generate the signal peptide, is indicated by an arrow.
Mentions: In the course of sequencing larger segments of an unstable genomic DNA region of S. lividans 66 WT (named within the text S. lividans WT) (Betzler et al., 1987), we discovered a reading frame of 1758 bp. This was subsequently (see below) named hyaS (EMBL, DS: 72304). The deduced protein, named HyaS (Fig. 1), comprises 585 amino acids (aa), including a signal peptide. It shares the highest (99%), second highest (73%) and third highest (63%) amino acid identity with, respectively, one hypothetical protein (including a signal peptide) deduced from the Streptomyces coelicolor A3(2) genomic sequence (Bentley et al., 2002), one from the Streptomyces griseus (Ohnishi et al., 2008) and one from the Streptomyces avermitilis genome (Ikeda et al., 2003). Furthermore, a slightly less related deduced protein (586 aa, including the predicted signal peptide) is encoded within the deposited genome of one Streptomyces scabies strain (Fig. 1). DNA–DNA hybridizations and analyses of PCR‐amplified fragments (data not shown) revealed the abundance of hyaS‐related sequences among six additionally tested Streptomyces species (see Experimental procedures).

Bottom Line: The HyaS protein is dominantly associated with the substrate hyphae.Investigations of ΔH transformants, each carrying a specifically mutated gene, lead to the conclusion that the in situ oxidase activity correlates with the pellet-inducing role of HyaS, and depends on the presence of certain histidine residues.These data present the first molecular basis for future manipulation of pellets, and concomitant production of secondary metabolites during biotechnological processes.

View Article: PubMed Central - PubMed

Affiliation: University of Osnabrück, FB Biology/Chemistry, Applied Genetics of Microorganisms, 49069 Osnabrück, Germany.

Show MeSH
Related in: MedlinePlus