Open AccessImmunological characterization of the Prochlorothrix hollandica and Prochloron sp. chlorophyll a / b antenna proteins
Author(s) -
Bullerjahn George S.,
Jensen Timothy C.,
Sherman Debra M.,
Sherman Louis A.
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb13844.x
Subject(s) - biology , thylakoid , polyclonal antibodies , prokaryote , fusion protein , antibody , chloroplast , escherichia coli , biochemistry , microbiology and biotechnology , gene , genetics , recombinant dna
Polyclonal antibodies were prepared against the major antenna chlorophyll (Chl) a / b ‐binding protein from the prokaryote Prochlorothrix hollandica (Burger‐Wiersma et al. (1986) Nature (Lond.) 320, 262–264). Immunoblotting experiments on Triton X‐114 phase‐partitioned P. hollandica thylakoids revealed that the antibody recognizes intrinsic membrane polypeptides of 33 and 30 kDa, and immunocytochemistry of P. hollandica thin sections showed that the antibody preferentially decorates the thylakoid. The antibody was immunopurified against a LacZ fusion protein produced in Escherichia coli by an immunopositive phage clone retrieved from a λZAP expression library. This purified antibody cross‐reacted to both the 33 and 30 kDa polypeptides, indicating that these proteins are either structurally related products of different genes, or modified forms of the same gene product. Whereas immunological crossreactivity of Prochlorothrix antibody to the major LHC‐II Chl a / b antenna of maize could not be detected, the immunopurified antibody reacted strongly to the major 34 kDa Chl a / b antenna protein from the prokaryote Prochloron sp. (Lewin (1975) Phycologia 14, 153–160). These data confirm the structural similarity of the prochlorophyte photosynthetic antenna systems.