Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724.
Proc Natl Acad Sci U S A. 1985 Jan;82(1):58-62. doi: 10.1073/pnas.82.1.58.
The light-harvesting II (LHII) structural genes coding for the (B800-B850 complex) beta- and alpha-polypeptides have been cloned and the nucleotide and deduced polypeptide sequences have been determined. This completes the sequencing of all seven structural genes coding for the structural polypeptides of the photosynthetic apparatus that bind the pigments and cofactors participating in the primary light reactions of photosynthesis. Unlike the structural genes coding for the reaction center L, M, and H subunits and the light-harvesting I (LHI) (B870 complex) structural polypeptides, the LHII structural genes are not within the 46-kilobase photosynthetic gene cluster carried by the R-prime plasmid pRPS404. Identical organization of the beta and alpha structural genes for both LHI and LHII and sequence homologies between the two beta-polypeptides and between the two alpha-polypeptides suggests that both complexes arose by gene duplication from a single ancestral light-harvesting complex and that the putative bacteriochlorophyll binding sequence Ala-X-X-X-His has been absolutely conserved.
已克隆编码(B800-B850 复合)β-和 α-多肽的集光 II(LHII)结构基因,并测定了核苷酸和推导的多肽序列。这完成了参与光合作用原初光反应的结合色素和辅因子的光合机构的结构多肽的所有七个结构基因的测序。与编码反应中心 L、M 和 H 亚基和集光 I(LHI)(B870 复合)结构多肽的结构基因不同,LHII 结构基因不在 R-prime 质粒 pRPS404 携带的 46 千碱基光合基因簇内。LHII 和 LHI 的β和α结构基因的相同组织以及两个β-多肽和两个α-多肽之间的序列同源性表明,这两个复合物都是由一个单一的祖先集光复合物通过基因复制产生的,并且假定的细菌叶绿素结合序列 Ala-X-X-X-His 已被绝对保守。