z-logo
open-access-imgOpen Access
Sequence homology between the 32K dalton and the D2 chloroplast membrane polypeptides of Chlamydomonas reinhardii
Author(s) -
JeanDavid Rochaix,
Michel Dron,
Michèle Rahire,
Pia Malnoë
Publication year - 1984
Publication title -
plant molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.448
H-Index - 174
eISSN - 1573-5028
pISSN - 0167-4412
DOI - 10.1007/bf00033383
Subject(s) - biology , homology (biology) , chlamydomonas , chloroplast , open reading frame , gene , genetics , thylakoid , genome , peptide sequence , mutant
The region of the chloroplast genome of Chlamydomonas reinhardii containing the gene of the thylakoid polypeptide D2 (psbD) has been sequenced. A unique open reading frame of 350 codons exists in this region. Because the first ATG is followed 11 codons downstream by a second one, the D2 polypeptide consists of either 339 or 350 amino acids. Comparison of the sequences of D2 and the 32K dalton polypeptides, both of which are associated with photosystem II, reveals partial homology. Although, the overall homology of these two polypeptides is only 27%, they contain several related regions and their hydropathic profiles are strikingly similar. These data suggest that the two polypeptides may have related functions and/or that their genes may have originated from a common ancestor. Alternatively, convergent evolution of these polypeptides may be due to structural constraints in the thylakoid membrane. Limited sequence homology is also observed between the D2 polypeptide and some of the subunits of the reaction centers of photosynthetic bacteria.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom