Occurrence and characterization of PEND proteins in angiosperms.
The PEND protein is a DNA-binding protein in the inner envelope membrane of the developing chloroplast. It consists of a short pre-sequence, an N-terminal DNA-binding domain (cbZIP), a central repeat domain, and a C-terminal transmembrane domain. PEND homologs have been detected in various angiosperms, including Arabidopsis thaliana, Brassica napus, Medicago truncatula, cucumber and cherry. Monocot homologs have also been detected in barley and rice, but sequence conservation was low in monocots. PEND-related sequences have not been detected in non-flowering plants and algae. Green fluorescent protein fusions consisting of the N-terminal as well as full-length PEND homologs in A. thaliana and B. napus were targeted to chloroplasts, and localized to nucleoids and chloroplast periphery, respectively. Immunoblot analysis suggested that crucifer homologs were present in chloroplasts probably as a dimer, as in the case of pea. These results suggest that PEND protein is present in angiosperms, and the homologs in crucifers are functionally analogous to the PEND protein in pea.
Terasawa
Kimihiro
K
Department of Molecular Biology, Faculty of Science, Saitama University, Sakura-ku, Saitama, 338-8570, Japan.
Sato
Naoki
N
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000737:chemistry; D050976:Basic-Leucine Zipper Transcription Factors; D001937:Brassica / Q000737:chemistry; D002736:Chloroplasts / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000032:analysis* / Q000737:chemistry / Q000235:genetics*; D019143:Evolution, Molecular; D019684:Magnoliopsida / Q000737:chemistry*; D008969:Molecular Sequence Data; D018515:Plant Leaves / Q000737:chemistry; D010940:Plant Proteins / Q000032:analysis* / Q000737:chemistry / Q000235:genetics*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D050976:Basic-Leucine Zipper Transcription Factors; D004268:DNA-Binding Proteins; C112640:PEND protein, plant; D010940:Plant Proteins