UNSPECIFIED. (2004) The archaeal Sec-dependent protein translocation pathway. PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES, 359 (1446). pp. 919-927. ISSN 0962-8436

Full text not available from this repository.

Abstract

Over the past three decades, transport of proteins across cellular membranes has been studied extensively in various model systems. One of the major transport routes, the so-called Sec pathway, is conserved in all domains of life. Very little is known about this pathway in the third domain of life, archaea. The core components of the archaeal, bacterial and eucaryal Sec machinery are similar, although the archacal components appear more closely related to their eucaryal counterparts. Interestingly, the accessory factors of the translocation machinery are similar to bacterial components, which indicates a unique hybrid nature of the archaeal translocase complex. The mechanism of protein translocation in archaea is completely unknown. Based on genomic sequencing data, the most likely system for archaeal protein translocation is similar to the eucaryal co-translational translocation pathway for protein import into the endoplasmic reticulum, in which a protein is pushed across the translocation channel by the ribosome. However, other models can also be envisaged, such as a bacterial-like system in which a protein is translocated posttranslationally with the aid of a motor protein analogous to the bacterial ATPase SecA. This review discusses the different models. Furthermore, an overview is given of some of the other components that may be involved in the protein translocation process, such as those required for protein targeting, folding and post-translational modification.

Item Type:	Journal Article
Subjects:	Q Science > QH Natural history > QH301 Biology
Journal or Publication Title:	PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES
Publisher:	ROYAL SOC LONDON
ISSN:	0962-8436
Date:	29 June 2004
Volume:	359
Number:	1446
Number of Pages:	9
Page Range:	pp. 919-927
Identification Number:	10.1098/rstb.2003.1461
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/8261

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item