title: Posttranslational protein modification in Archaea.
abstract: One of the first hurdles to be negotiated in the postgenomic era involves the description of the entire protein content of the cell, the proteome. Such efforts are presently complicated by the various posttranslational modifications that proteins can experience, including glycosylation, lipid attachment, phosphorylation, methylation, disulfide bond formation, and proteolytic cleavage. Whereas these and other posttranslational protein modifications have been well characterized in Eucarya and Bacteria, posttranslational modification in Archaea has received far less attention. Although archaeal proteins can undergo posttranslational modifications reminiscent of what their eucaryal and bacterial counterparts experience, examination of archaeal posttranslational modification often reveals aspects not previously observed in the other two domains of life. In some cases, posttranslational modification allows a protein to survive the extreme conditions often encountered by Archaea. The various posttranslational modifications experienced by archaeal proteins, the molecular steps leading to these modifications, and the role played by posttranslational modification in Archaea form the focus of this review.
authors.affiliation: Dept. of Life Sciences, Ben Gurion University, P.O. Box 653, Beersheva 84105, Israel. jeichler@bgu.ac.il
authors.forename: Jerry
authors.initials: J
authors.lastname: Eichler
authors.forename: Michael W W
authors.initials: MW
authors.lastname: Adams
mesh_terms: D001105:Archaea / Q000235:genetics / Q000378:metabolism*; D019843:Archaeal Proteins / Q000235:genetics / Q000378:metabolism*; D002240:Carbohydrate Sequence; D004220:Disulfides / Q000378:metabolism; D006031:Glycosylation; D008074:Lipoproteins / Q000378:metabolism; D008745:Methylation; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational / Q000502:physiology*
chemical_list: D019843:Archaeal Proteins; D004220:Disulfides; D008074:Lipoproteins