大肠杆菌胞壁质中肽交联桥的裂解与再合成
Cleavage and resynthesis of peptide cross bridges in Escherichia coli murein.
作者信息
Goodell E W, Schwarz U
出版信息
J Bacteriol. 1983 Oct;156(1):136-40. doi: 10.1128/jb.156.1.136-140.1983.
Abstract
In Escherichia coli, peptide cross bridges in the murein undergo turnover after they are synthesized. Peptide cross bridges formed in the presence of [3H]diaminopimelic acid were found to lose 3H label from their donor peptides after the [3H]diaminopimelic acid was removed from the growth medium. There was a corresponding increase in the amount of 3H label in acceptor peptides so that the total amount of label in the peptide cross bridges remained constant. Our explanation of this observation is that the cross bridges are cleaved by the cell, and the original 3H-labeled donor peptides are incorporated into new cross bridges. Since these 3H-labeled peptides are now only tetrapeptides, they can only be used as acceptors when new cross bridges are formed.
摘要
在大肠杆菌中，胞壁质中的肽交联桥在合成后会发生周转。发现在[3H]二氨基庚二酸存在下形成的肽交联桥，当从生长培养基中去除[3H]二氨基庚二酸后，其供体肽会失去3H标记。受体肽中的3H标记量相应增加，使得肽交联桥中的总标记量保持恒定。我们对这一观察结果的解释是，交联桥被细胞裂解，原来带有3H标记的供体肽被并入新的交联桥中。由于这些带有3H标记的肽现在只是四肽，当形成新的交联桥时，它们只能用作受体。
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