The Streptomyces reticuli α-chitin-binding protein CHB2 and its gene
The Streptomyces reticuli α-chitin-binding protein CHB2 and its gene
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DOI：
10.1099/00221287-144-5-1291
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发表时间：
1998-05-01
期刊：
影响因子：
2.8
通讯作者：
Schrempf, H
中科院分区：
文献类型：
--
作者：
Kolbe, S;Fischer, S;Schrempf, H
当与含几丁质的真菌共培养时，网状链霉菌分泌几丁质结合蛋白CHB 2。显微镜和免疫学研究表明，CHB 2像胶水一样介导真菌和链霉菌菌丝之间的接触。将CHB 2纯化至均一，并测定其N-末端氨基酸的序列并用于推导寡核苷酸，然后将其用于探针亚基因组文库。chb 2基因被克隆，测序和过表达。推导的成熟蛋白分子量为18.6 kDa，其大量氨基酸与橄榄绿链霉菌CHB 1的氨基酸相同。CHB 2有效地靶向不同类型的α-几丁质，但不靶向其他多糖。与纯化的蟹壳几丁质结合的解离常数（K-d，）为0.27 μ M。免疫学研究表明，CHB 1和CHB 2的同系物分泌链霉菌，而在存在的α-几丁质含底物的生长。
When co-cultivated with chitin-containing fungi, Streptomyces reticuli secretes the chitin-binding protein CHB2. Microscopical and immunological investigations revealed that CHB2 acts like a glue to mediate the contact between the fungal and the Streptomyces hyphae. CHB2 was purified to homogeneity, and the sequence of its N-terminal amino acids was determined and used to deduce an oligonucleotide, which was then used to probe a subgenomic library. The chb2 gene was cloned, sequenced and overexpressed. The deduced mature protein has a molecular mass of 18.6 kDa, and a large number of its amino acids are identical to those of CHB1 from Streptomyces olivaceoviridis. CHB2 effectively targets different types of a-chitin, but no other polysaccharide. The dissociation constant (K-d,) for binding to purified crab shell chitin is 0.27 mu M. Immunological studies suggest that homologues of CHB1 and CHB2 are secreted by streptomycetes while growing in the presence of alpha-chitin-containing substrates.