Identification of two structurally related proteins involved in proteolytic processing of precursors targeted to the chloroplast.
AUTOR(ES)
Oblong, J E
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=557014Documentos Relacionados
- Two viral proteins involved in the proteolytic processing of the cowpea mosaic virus polyproteins.
- Processing of the precursor to a chloroplast ribosomal protein made in the cytosol occurs in two steps, one of which depends on a protein made in the chloroplast.
- Translational regulation in the chloroplast.
- Two proteins targeted to the same lytic granule compartment undergo very different posttranslational processing.
- Vaccinia Virus Encodes Two Proteins That Are Structurally Related to Members of the Plasma Serine Protease Inhibitor Superfamily