Abstract

CONTENT ALERTS Receive: RSS Feeds, eTOCs, free email alerts (when new articles cite this article), more» Information about commercial reprint orders: http://jb.asm.org/site/misc/reprints.xhtml To subscribe to to another ASM Journal go to: http://journals.asm.org/site/subscriptions/ JOURNAL OF BACTERIOLOGY, Mar. 1995, p. 1123–1128 0021-9193/95/$04.00 0 Copyright 1995, American Society for Microbiology Vol. 177, No. 5 IAIN C. SUTCLIFFE* AND ROY R. B. RUSSELL Department of Oral Biology, The Dental School, University of Newcastle upon Tyne, Framlington Place, Newcastle upon Tyne NE2 4BW, United Kingdom INTRODUCTION Our view of the complexity of the Gram-positive bacterial cell envelope has altered considerably in recent years, with the recognition of the presence of a variety of proteins retained by different mechanisms. Lipoproteins, i.e., proteins containing lipid covalently linked to an N-terminal cysteine residue, have been extensively studied in gram-negative bacteria (7), but examples from gram-positive species have only quite recently been recognized (Table 1). Despite its thickness, the peptidoglycan layer of gram-positive bacteria remains a relatively porous structure. Thus, in the absence of the retentive outer membrane, components carrying out functions within the gram-positive cell envelope must somehow be tethered in order to prevent their loss into the growth environment. The lipidated N terminus is presumed