{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["181(24)"],"submitter":["Bormann C"],"pubmed_abstract":["The afp1 gene, which encodes the antifungal protein AFP1, was cloned from nikkomycin-producing Streptomyces tendae Tü901, using a nikkomycin-negative mutant as a host and screening transformants for antifungal activity against Paecilomyces variotii in agar diffusion assays. The 384-bp afp1 gene has a low G+C content (63%) and a transcription termination structure with a poly(T) region, unusual attributes for Streptomyces genes. AFP1 was purified from culture filtrate of S. tendae carrying the afp1 gene on the multicopy plasmid pIJ699. The purified protein had a molecular mass of 9,862 Da and lacked a 42-residue N-terminal peptide deduced from the nucleotide sequence. AFP1 was stable at extreme pH values and high temperatures and toward commercial proteinases. AFP1 had limited similarity to"],"journal":["Journal of bacteriology"],"pagination":["7421-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC94197"],"repository":["biostudies-literature"],"pubmed_title":["Characterization of a novel, antifungal, chitin-binding protein from Streptomyces tendae Tu901 that interferes with growth polarity."],"pmcid":["PMC94197"],"pubmed_authors":["Jung G","Baier D","Bormann C","Berger J","Schwarz H","Raps C","Horr I"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of a novel, antifungal, chitin-binding protein from Streptomyces tendae Tu901 that interferes with growth polarity.","description":"The afp1 gene, which encodes the antifungal protein AFP1, was cloned from nikkomycin-producing Streptomyces tendae Tü901, using a nikkomycin-negative mutant as a host and screening transformants for antifungal activity against Paecilomyces variotii in agar diffusion assays. The 384-bp afp1 gene has a low G+C content (63%) and a transcription termination structure with a poly(T) region, unusual attributes for Streptomyces genes. AFP1 was purified from culture filtrate of S. tendae carrying the afp1 gene on the multicopy plasmid pIJ699. The purified protein had a molecular mass of 9,862 Da and lacked a 42-residue N-terminal peptide deduced from the nucleotide sequence. AFP1 was stable at extreme pH values and high temperatures and toward commercial proteinases. AFP1 had limited similarity to","dates":{"release":"1999-01-01T00:00:00Z","publication":"1999 Dec","modification":"2025-04-05T07:10:30.208Z","creation":"2019-03-27T00:18:34Z"},"accession":"S-EPMC94197","cross_references":{"pubmed":["10601197"],"doi":["10.1128/JB.181.24.7421-7429.1999"]}}