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GrainGenes Reference Report: PMB-13-583

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Reference	PMB-13-583
Title	Transiently expressed early light-inducible thylakoid proteins share transmembrane domains with light-harvesting chlorophyll binding proteins
Journal	Plant Molecular Biology
Year	1989
Volume	13
Pages	583-594
Author	Grimm B Kruse E Kloppstech K
Type	Article
Language	English
Abstract	The early light-inducible proteins (ELIPs) of barley chloroplasts are encoded in two multigene families yielded end products of different molecular mass. Sequencing of complete cDNA clones showed that the low and high molecular mass proteins differ by the presence or absence of a 65 amino acid peptide in the amino-terminal part of themature proteins. Two domains of the ELIPs reveal striking similarity in amino acid sequence with two transmembrane domains of all known light-harvesting chlorophyll a/b-binding proteins from photosystem I and Ii may be of importance in anchoring the polypeptides in the membrane. The cDNA sequences of two low molecular mass ELIPs differ by an insert of 5 codons in the putative transit peptide. By in vitro transcription and translation of the cloned DNA and subsequent transport of the products into chloroplasts it could be established that the two precursors are processed into products of identical apparent molecular mass. In vitro translated ELIPs were incorporated into thylakoid membranes both as precursors and mature polypeptides. It is suggested that ELIPs are pigment-free substitutes for light-harvesting polypeptides in the assembly of photosynthetic units during early development of thylakoids.
Probe	HV 58 HV 60 HV 90
Keyword	[ Hide all but 1 of 17 ] Amino acid sequence Complementary dna Cultivar Aramir DDBJ-X15691 DDBJ-X15692 DDBJ-X15693 EMBL- X15691 EMBL-X15692 EMBL-X15693 GENBANK-X15691 GENBANK-X15692 GENBANK-X15693 Hordeum-vulgare Molecular sequence data Nucleotide sequence Photosystem I Photosystem II

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