@article{mbs:/content/journal/micro/10.1099/00221287-144-4-1077, author = "Morita, Masashi", title = "Molecular analysis of Physarum haemagglutinin l: lack of a signal sequence, sulphur amino acids and post-translational modifications", journal= "Microbiology", year = "1998", volume = "144", number = "4", pages = "1077-1084", doi = "https://doi.org/10.1099/00221287-144-4-1077", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-144-4-1077", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "lectin", keywords = "post-translational modification", keywords = "Physarum polycephalum", keywords = "cDNA cloning", keywords = "haemagglutinin", abstract = "The cDNAs encoding haemagglutinin I from plasmodia of Physarum polycephalum have been cloned using PCR protocols. The composite haemagglutinin I cDNA sequence, derived from several overlapping clones from PCR fragments, spans 408 nt and the 315 bp ORF encodes a polypeptide of 104 aa without a typical signal sequence. The putative molecular mass deduced from the amino acid sequence (10760.76 Da) corresponds exactly to that determined by electrospray ionization MS (10759.86±.15 Da), suggesting that haemagglutinin I is not subject to post-translational modification. Haemagglutinin I lacks sulphur amino acids and has a β-sheet as the major secondary structure. Expression of the coding sequence in Escherichia coli yielded a product that exhibits the same sugar-binding specificity as natural haemagglutinin I. The deduced amino acid sequence shows little similarity to that of any known lectins and thus apparently represents a novel type of lectin.", }