Nova Publishers
My Account Nova Publishers Shopping Cart
HomeBooksSeriesJournalsReference CollectionseBooksInformationSalesImprintsFor Authors
            
  Top » Catalog » Books » Biology » Microbiology » Archaea: Structure, Habitats and Ecological Significance Chapters » My Account  |  Cart Contents  |  Checkout   
Quick Find
  
Use keywords to find the product you are looking for.
Advanced Search
What's New? more
Fetal Alcohol Syndrome: Recognition, Differential Diagnosis and Long-Term Effects
$82.00
Shopping Cart more
0 items
Information
Shipping & Returns
Privacy Notice
Conditions of Use
Contact Us
Notifications more
NotificationsNotify me of updates to The Archaeal Flagellum: A Novel Prokaryotic Motility Structure and the Role of Posttranslational Modifications in its Assembly and Function pp. 1-37
Tell A Friend
 
Tell someone you know about this product.
The Archaeal Flagellum: A Novel Prokaryotic Motility Structure and the Role of Posttranslational Modifications in its Assembly and Function pp. 1-37 $100.00
Authors:  (Ken F. Jarrell, Department of Microbiology and Immunology, Queen’s University, Kingston, Ontario, Canada)
Abstract:
The archaeal flagellum is a unique prokaryotic motility apparatus responsible for swimming that is found in all of the major cultured subgroupings of Archaea. While they are rotating structures like bacterial flagella, archaeal flagella nevertheless differ from their bacterial namesake in several fundamental ways. Indeed, archaeal flagella have more similarities to bacterial type IV pili, organelles responsible for a type of surface motility called twitching. Structurally, archaeal flagella are thinner than bacterial flagella and lack an internal channel large enough to allow passage of subunits. The flagellins in archaea are made as preproteins with type IV pilin-like signal peptides which are removed by a dedicated preflagellin peptidase homologous to the bacterial type IV prepilin peptidase. Both enzymes belong to a novel family of aspartic acid proteases with conserved aspartic acid residues that are necessary for signal peptide cleavage. Bacterial flagellins, on the other hand, are never made with signal peptides. Additional homologues have been identified between the archaeal flagella system and the type IV pilus system, including a conserved ATPase and a membrane component. A further posttranslational modification commonly found on archaeal flagellins is attachment of an N-linked glycan. This is again never seen in bacterial flagellins which can be, in rare cases, glycoproteins but always with the glycan attached in an O-linkage. Much recent data has accumulated on the assembly, biosynthesis and attachment of the N-glycan to archaeal flagellins and the important role that the glycan plays in flagella assembly and function. 


Available Options:
Version:
This Item Is Currently Unavailable.
Special Focus Titles
01.Violent Communication and Bullying in Early Childhood Education
02.Cultural Considerations in Intervention with Women and Children Exposed to Intimate Partner Violence
03.Chronic Disease and Disability: The Pediatric Lung
04.Fruit and Vegetable Consumption and Health: New Research
05.Fire and the Sword: Understanding the Impact and Challenge of Organized Islamism. Volume 2

Nova Science Publishers
© Copyright 2004 - 2020

The Archaeal Flagellum: A Novel Prokaryotic Motility Structure and the Role of Posttranslational Modifications in its Assembly and Function pp. 1-37