Accession Number:

ADA210527

Title:

Molecular Mechanisms of Chemosensory Receptors, Signal Transducers, and the Activation of Gene Expression Controlling Establishment of a Marine Symbiosis

Descriptive Note:

Annual rept. 1 Aug 1988-31 Jul 1989

Corporate Author:

CALIFORNIA UNIV SANTA BARBARA MARINE SCIENCE INST

Personal Author(s):

• Morse, Daniel E.

Report Date:

1989-07-01

Pagination or Media Count:

7.0

Abstract:

We have resolved and analyzed in vitro 10 of the 13 separate molecular reactions and pathways controlling metamorphosis of Haliotis larvae in response to exogenous signal molecules that we first identified in vivo. Two different chemosensory receptors and receptor-dependent signal transduction cascades regulating metamorphosis have now been characterized on highly purified cilia from the larval epithelium. The receptors, a receptor-regulated G protein, and proteins phosphorylated by receptor-regulated protein kinases A and C have been labeled in vitro, and the latter three labeled proteins have been purified. Three additional proteins have been characterized, and shown to be developmentally regulated in the metamorphosis of Haliotis larvae. The cDNA for one of these, a novel serine protease, has been cloned and sequenced. Deductions about the structure and function of the enzyme based on the nucleic acid sequence analysis have been confirmed by measurements of the catalytic properties of the enzyme.

Descriptors:

• *TRANSDUCERS
• *CHEMORECEPTORS
• *METAMORPHOSIS
• *ACTIVATION
• *REACTION KINETICS
• *LARVAE
• *CATALYSIS
• *SIGNALS
• *NUCLEIC ACIDS
• MOLECULAR PROPERTIES
• CHEMICAL ANALYSIS
• PEPTIDE HYDROLASES
• SERINE
• CILIA
• IN VIVO ANALYSIS
• CLONES
• GENES
• PURIFICATION
• SEQUENCES
• IN VITRO ANALYSIS
• PROTEINS
• ENZYMES
• MOLECULES
• EPITHELIUM

Subject Categories:

• Biochemistry
• Genetic Engineering and Molecular Biology
• Biology
• Anatomy and Physiology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE