TY - JOUR
T1 - Composition and structure of photosystem I in the moss Physcomitrella patens
AU - Busch, Andreas
AU - Petersen, Jørgen
AU - Webber-Birungi, Miriam T.
AU - Powikrowska, Marta
AU - Lassen, Lærke Marie Münter
AU - Naumann-Busch, Bianca
AU - Nielsen, Agnieszka Janina Zygadlo
AU - Ye, Juanying
AU - Boekema, Egbert J.
AU - Jensen, Ole Nørregaard
AU - Lunde, Christina
AU - Jensen, Poul Erik
PY - 2013/7
Y1 - 2013/7
N2 - Recently, bryophytes, which diverged from the ancestor of seed plants more than 400 million years ago, came into focus in photosynthesis research as they can provide valuable insights into the evolution of photosynthetic complexes during the adaptation to terrestrial life. This study isolated intact photosystem I (PSI) with its associated light-harvesting complex (LHCI) from the moss Physcomitrella patens and characterized its structure, polypeptide composition, and light-harvesting function using electron microscopy, mass spectrometry, biochemical, and physiological methods. It became evident that Physcomitrella possesses a strikingly high number of isoforms for the different PSI core subunits as well as LHCI proteins. It was demonstrated that all these different subunit isoforms are expressed at the protein level and are incorporated into functional PSI-LHCI complexes. Furthermore, in contrast to previous reports, it was demonstrated that Physcomitrella assembles a light-harvesting complex consisting of four light-harvesting proteins forming a higher-plant-like PSI superstructure.
AB - Recently, bryophytes, which diverged from the ancestor of seed plants more than 400 million years ago, came into focus in photosynthesis research as they can provide valuable insights into the evolution of photosynthetic complexes during the adaptation to terrestrial life. This study isolated intact photosystem I (PSI) with its associated light-harvesting complex (LHCI) from the moss Physcomitrella patens and characterized its structure, polypeptide composition, and light-harvesting function using electron microscopy, mass spectrometry, biochemical, and physiological methods. It became evident that Physcomitrella possesses a strikingly high number of isoforms for the different PSI core subunits as well as LHCI proteins. It was demonstrated that all these different subunit isoforms are expressed at the protein level and are incorporated into functional PSI-LHCI complexes. Furthermore, in contrast to previous reports, it was demonstrated that Physcomitrella assembles a light-harvesting complex consisting of four light-harvesting proteins forming a higher-plant-like PSI superstructure.
U2 - 10.1093/jxb/ert126
DO - 10.1093/jxb/ert126
M3 - Journal article
C2 - 23682117
SN - 0022-0957
VL - 64
SP - 2689
EP - 2699
JO - Journal of Experimental Botany
JF - Journal of Experimental Botany
IS - 10
ER -