Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



ID: 318533.0, MPI für Biochemie / Structural Biology (W. Baumeister)
The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum
Authors:Ruepp, A.; Graml, W.; Santos-Martinez, M. L.; Koretle, K. K.; Volker, C.; Mewes, H. W.; Frishman, D.; Stocker, S.; Lupas, A. N.; Baumeister, W.
Date of Publication (YYYY-MM-DD):2000
Title of Journal:Nature
Journal Abbrev.:Nature
Volume:407
Issue / Number:6803
Start Page:508
End Page:513
Audience:Not Specified
Abstract / Description:Thermoplasma acidophilum is a thermoacidophilic archaeon that thrives at 59 degrees C and pH 2, which was isolated from self-heating coal refuse piles and solfatara fields(1,2). Species of the genus Thermoplasma do not possess a rigid cell wall, but are only delimited by a plasma membrane. Many macromolecular assemblies from Thermoplasma, primarily proteases and chaperones, have been pivotal in elucidating the structure and function of their more complex eukaryotic homologues(3,4). Our interest in protein folding and degradation led us to seek a more complete representation of the proteins involved in these pathways by determining the genome sequence of the organism. Here we have sequenced the 1,564,905-base-pair genome in just 7,855 sequencing reactions by using a new strategy. The 1,509 open reading frames identify Thermoplasma as a typical euryarchaeon with a substantial complement of bacteria-related genes; however, evidence indicates that there has been much lateral gene transfer between Thermoplasma and Sulfolobus solfataricus, a phylogenetically distant crenarchaeon inhabiting the same environment. At least 252 open reading frames, including a complete protein degradation pathway and various transport proteins, resemble Sulfolobus proteins most closely. [References: 30]
Free Keywords:Protein; Expression; Glucose; Machine; Vat.; Multidisciplinary in Current Contents(R)/Agricultural, Biology & Environmental Sciences. Multidisciplinary in Current Contents(R)/Life Sciences. Multidisciplinary in Current Contents(R)/Physical, Chemical & Earth Sciences.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.