Minicoliagen-15, a novel minicollagen isolated from hydra, forms tubule structures in nematocysts

Patrizia Adamczyk, Sebastian Meier, Thomas Gross, Bert Hobmayer, Stephan Grzesiek, Hans Peter Baechinger, Thomas W. Holstein, Suat Oezbek

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Minicollagens constitute a family of unusually short collagen molecules isolated from cnidarians. They are restricted to the nematocyst, a cylindrical explosive organelle serving in defense and capture of prey. The nematocyst capsule contains a long tubule inside of its matrix, which is expelled and everted during an ultrafast discharge process. Here, we report the cloning and characterization of a novel minicollagen in Hydra, designated minicollagen-15 (NCol-15). NCol-15, like NCol-3 and NCol-4, shows deviations from the canonical cysteine pattern in its terminal cysteine-rich domains (CRDs). Minicollagens share common domain architectures with a central collagen sequence flanked by polyproline stretches and short N- and C-terminal CRDs. The CRDs are involved in the formation of a highly resistant cysteine network, which constitutes the basic structure of the nematocyst capsule. Unlike NCol-1, which is part of the capsule wall, NCol-15 is localized to tubules, arguing for a functional differentiation of minicollagens within the nematocyst architecture. NMR analysis of the altered C-terminal CRD of NCol-15 showed a novel disulfide-linked structure within the cysteine-containing region exhibiting similar folding kinetics and stability as the canonical CRDs. Our data provide evidence for evolutionary diversification among minicollagens, which probably facilitated alterations in the morphology of the nematocyst wall and tubule. (C) 2007 Elsevier Ltd. All rights reserved.
Original languageEnglish
JournalJournal of Molecular Biology
Volume376
Issue number4
Pages (from-to)1008-1020
ISSN0022-2836
DOIs
Publication statusPublished - 2008
Externally publishedYes

Keywords

  • Amino Acid Sequence
  • Animal Structures
  • Animals
  • Blotting, Western
  • Cloning, Molecular
  • Collagen
  • Disulfides
  • Dithiothreitol
  • Hydra
  • Immunohistochemistry
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Protein Folding
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Protein Transport
  • Proteins
  • Solutions
  • spinalin
  • 9007-34-5 Collagen
  • T8ID5YZU6Y Dithiothreitol
  • collagen
  • cysteine
  • disulfide
  • minicollagen n col 15
  • minicollagen ncol 3
  • minicollagen ncol 4
  • unclassified drug
  • article
  • cell organelle
  • cloning
  • coelenterate
  • embryo
  • human
  • human cell
  • nematocyst
  • nonhuman
  • nuclear magnetic resonance
  • priority journal
  • protein folding
  • protein localization
  • Cnidaria
  • cysteine-rich domain
  • evolution
  • minicollagen
  • BIOCHEMISTRY
  • DISULFIDE LINKAGE
  • CHEMICAL-SHIFT
  • NMR STRUCTURE
  • PROTEIN
  • DOMAIN
  • WALL
  • COLLAGENS
  • EVOLUTION
  • ALIGNMENT
  • PEPTIDES
  • protein folding kinetics
  • protein stability
  • Invertebrata Animalia (Animals, Invertebrates) - Cnidaria [41000] Hydra genus
  • minicollagen-15 cysteine-rich domain
  • 01500, Evolution
  • 02502, Cytology - General
  • 02506, Cytology - Animal
  • 10060, Biochemistry studies - General
  • 64008, Invertebrata: comparative, experimental morphology, physiology and pathology - Cnidaria
  • cloning laboratory techniques, genetic techniques
  • nuclear magnetic resonance laboratory techniques, spectrum analysis techniques
  • Biochemistry and Molecular Biophysics
  • Cell Biology
  • Methods and Techniques

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