Publication Type	Academic Article
Authors	Tessier L, Jallat S, Sauvageot M, Crystal R, Courtney M
Journal	FEBS Lett
Volume	208
Issue	2
Pagination	183-8
Date Published	11/24/1986
ISSN	0014-5793
Keywords	Escherichia coli, alpha 1-Antitrypsin
Abstract	Analysis of a series of lambda cII::alpha 1-antitrypsin (alpha 1AT) gene fusions of different sizes showed that increased alpha 1AT expression correlated with the stabilisation of a particular computer-predicted RNA secondary structure. Moreover, significant synthesis of unfused alpha 1AT was achieved by reconstruction of this conformation to permit interaction between the upstream region of the ribosome-binding site and the first part of the alpha 1AT coding sequence. This high-level expression was dependent upon certain silent point mutations in the coding sequence, indicating that RNA primary and secondary structure determinants can operate in concert to dictate the efficiency of protein synthesis.
DOI	10.1016/0014-5793(86)81014-6
PubMed ID	2946602