Identification of two structurally related proteins involved in proteolytic processing of precursors targeted to the chloroplast

Two proteins of 145 and 143 kDa were identified in pea which co-purify with a chloroplast processing activity that cleaves the precursor for the major light-harvesting chlorophyll binding protein (preLHCP). Antiserum generated against the 145/143 kDa doublet recognizes only these two polypeptides in...

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Bibliographic Details
Published in:The EMBO journal 1992-12, Vol.11 (12), p.4401-4409
Main Authors: Oblong, J.E, Lamppa, G.K
Format: Article
Language:English
Subjects:
activity
binding proteins
Biological and medical sciences
Biological Transport
Blotting, Western
Cell structures and functions
Centrifugation, Density Gradient
chlorophyll
chloroplast processing enzyme
Chloroplast, photosynthetic membrane and photosynthesis
chloroplasts
Chloroplasts - metabolism
Electrophoresis, Polyacrylamide Gel
enzyme activity
Epitopes
Fabaceae - chemistry
Fundamental and applied biological sciences. Psychology
Hydrolysis
identification
light harvesting complex
Molecular and cellular biology
Molecular Weight
Pisum sativum
Plant Proteins - chemistry
Plant Proteins - immunology
Plant Proteins - metabolism
Plants, Medicinal
precursors
processing
Protein Conformation
Protein Precursors - metabolism
Protein Processing, Post-Translational
protein transport
proteinases
proteins
proteolysis
purification
Substrate Specificity
Triticum - chemistry
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Summary:Two proteins of 145 and 143 kDa were identified in pea which co-purify with a chloroplast processing activity that cleaves the precursor for the major light-harvesting chlorophyll binding protein (preLHCP). Antiserum generated against the 145/143 kDa doublet recognizes only these two polypeptides in a chloroplast soluble extract. In immunodepletion experiments the antiserum removed the doublet, and there was a concomitant loss of cleavage of preLHCP as well as of precursors for the small subunit of Rubisco and the acyl carrier protein. The 145 and 143 kDa proteins co-eluted in parallel with the peak of processing activity during all fractionation procedures, but they were not detectable as a homo- or heterodimeric complex. The 145 and 143 kDa proteins were used separately to affinity purify immunoglobulins; each preparation recognized both polypeptides, indicating that they are antigenically related. Wheat chloroplasts contain a soluble species similar in size to the 145/143 kDa doublet.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1992.tb05540.x