NDLI: The presequence of Euglena LHCPII, a cytoplasmically synthesized chloroplast protein, contains a functional endoplasmic reticulum-targeting domain.

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The presequence of Euglena LHCPII, a cytoplasmically synthesized chloroplast protein, contains a functional endoplasmic reticulum-targeting domain.

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The presequence of Euglena LHCPII, a cytoplasmically synthesized chloroplast protein, contains a functional endoplasmic reticulum-targeting domain.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kishore, R. Schwartzbach, S. D. Muchhal, U. S.
Description	Author Affiliation: Kishore R ( School of Biological Sciences, University of Nebraska, Lincoln 68588.);
Abstract	The precursor to the Euglena light-harvesting chlorophyll a/b-binding protein of photosystem II (pLHCPII) is unique; it is a polyprotein, synthesized on membrane-bound ribosomes and transported to the Golgi apparatus prior to chloroplast localization. A cDNA corresponding to the 5' end of LHCPII mRNA has been isolated and sequenced. The deduced amino acid sequence of this cDNA indicates that Euglena pLHCPII contains a 141-amino acid N-terminal extension. The N-terminal extension contains three hydrophobic domains and a potential signal peptidase cleavage site at amino acid 35. Cotranslational processing by canine microsomes removed approximately 35 amino acids from an in vitro synthesized 33-kDa pLHCPII composed of a 141-amino acid N-terminal extension and a 180-amino acid partial LHCPII unit truncated at the beginning of the third membrane-spanning hydrophobic domain. Processed pLHCPII was degraded by exogenous protease, indicating that it had not been translocated to the microsomal lumen. Extraction with 0.1 M Na2CO3, pH 11.5, did not remove the processed pLHCPII from the microsomal membrane. A stop-transfer membrane anchor sequence appears to anchor the nascent protein within the membrane, preventing translocation into the lumen. Taken together, these results provide biochemical evidence for a functional cleaved signal sequence within the N-terminal extension of a Euglena cytoplasmically synthesized chloroplast-localized protein.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	24
Volume Number	90
Language	English
Publisher	National Academy of Sciences
Publisher Date	1993-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Apoproteins Biosynthesis Endoplasmic Reticulum Metabolism Euglena Photosynthetic Reaction Center Complex Proteins Photosystem II Protein Complex Plant Proteins Protein Precursors Protozoan Proteins Amino Acid Sequence Animals Cloning, Molecular Conserved Sequence Intracellular Membranes Light-Harvesting Protein Complexes Microsomes Molecular Sequence Data Oligodeoxyribonucleotides Protein Sorting Signals RNA, Messenger Sequence Homology, Amino Acid Transcription, Genetic Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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