Differences between Saccharomyces cerevisiae and Bacillus subtilis in secretion of human lysozyme

Occurrence of S‐(1,2‐dicarboxyethyl)‐cysteine at position 77 in mutant human lysozyme secreted by Saccharomyces cerevisiae

“…Recently, Yoshimura et al [2] and Jigami et al [3] have reported the secretion of human lysozyme in a native form by Succhuromyces cerevisiue. The use of this system has made it possible for us to purify and crystallize the recombinant human lysozyme [2] and to engineer and analyze human lyozyme in studying the secretion mechanism [4 -61, structure/function relationship [7, 81 and the process of protein folding in vivo Previously, when Val1 10 of human lysozyme was replaced with Pro to alter substrate specificity, a mutant Pii0 (VallIO+Pro) was obtained which consisted of four proteins (A, B, C and D) on final puification [7]. D (designated Plio-D) has been found to contain four disulfide bonds in the correct positions for native human lysozyme when subjected to X-ray structure analysis (unpublished results).…”

Protein Traffic for Secretion and Related Machinery ofBacillus subtilis

“…98) In contrast, the amount of human proteins such as serum albumin and lysozyme produced in B. subtilis is very low. 99,100) We also tested extracellular production of human hepatitis B virus preS2 antigen and human angiotensin I as hybrid proteins with B. subtilis -amylase. B. subtilis -amylase (AmyE) consists of 660 amino acids, including its signal peptide and prosequence.…”

Construction of a divalent cell adhesive lysozyme by introducing the Arg‐Gly‐Asp sequence at two sites

“…Mutant human lysozymes were expressed in yeast as described previously [10]. Secreted mutant lysozymes were purified essentially as described [9].…”