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偶然的变异性?非脊椎动物珠蛋白的氨基酸序列。

Adventitious variability? The amino acid sequences of nonvertebrate globins.

作者信息

Vinogradov S N, Walz D A, Pohajdak B, Moens L, Kapp O H, Suzuki T, Trotman C N

机构信息

Department of Biochemistry, Wayne State University School of Medicine, Detroit, MI 48201.

出版信息

Comp Biochem Physiol B. 1993 Sep;106(1):1-26. doi: 10.1016/0305-0491(93)90002-m.

DOI:10.1016/0305-0491(93)90002-m
PMID:8403841
Abstract
  1. The more than 140 amino acid sequences of non-vertebrate hemoglobins (Hbs) and myoglobins (Mbs) that are known at present, can be divided into several distinct groups: (1) single-chain globins, containing one heme-binding domain; (2) truncated, single-chain, one-domain globins; (3) chimeric, one-domain globins; (4) chimeric, two-domain globins; and (5) chimeric multi-domain globins. 2. The crystal structures of eight nonvertebrate Hbs and Mbs are known, all of them monomeric, one-domain globin chains. Although these molecules represent plants, prokaryotes and several metazoan groups, and although the inter-subunit interactions in the dimeric and tetrameric molecules differ from the ones observed in vertebrate Hbs, the secondary structures of all seven one-domain globins retain the characteristic vertebrate "myoglobin fold". No crystal structures of globins representing the other four groups have been determined. 3. Furthermore, a number of the one-, two- and multi-domain globin chains participate in a broad variety of quaternary structures, ranging from homo- and heterodimers to highly complex, multisubunit aggregates with M(r) > 3000 kDa (S. N. Vinogradov, Comp. Biochem. Physiol. 82B, 1-15, 1985). 4. (1) The single-chain, single-domain globins are comparable in size to the vertebrate globins and exhibit the widest distribution. (A) Intracellular Hbs include: (i) the monomeric and polymeric Hbs of the polychaete Glycera; (ii) the tetrameric Hb of the echiuran Urechis; (iii) the dimeric Hbs of echinoderms such as Paracaudina and Caudina; and (iv) the dimeric and tetrameric Hbs of molluscs, the bivalves Scapharca, Anadara, Barbatia and Calyptogena. (B) Extracellular Hbs include: (i) the multiple monomeric and dimeric Hbs of the larva of the insect Chironomus; (ii) the Hbs of nematodes such as Trichostrongylus and Caenorhabditis; (iii) the globin chains forming tetramers and dodecamers and comprising approximately 2/3 of the giant (approximately 3600 kDa), hexagonal bilayer (HBL) Hbs of annelids, e.g. the oligochaete Lumbricus and the polychaete Tylorrhynchus and of the vestimentiferan Lamellibrachia; and (iv) the globin chains comprising the ca 400 kDa Hbs of Lamellibrachia and the pogonophoran Oligobrachia. (C) Cytoplasmic Hbs include: (i) the Mbs of molluscs, the gastropods Aplysia, Bursatella, Cerithedea, Nassa and Dolabella and the chiton Liolophura; (ii) the three Hb of the symbiont-harboring bivalve Lucina; (iii) the dimeric Hb of the bacterium Vitreoscilla; and (iv) plant Hbs, including the Hbs of symbiont-containing legumes (Lgbs), the Hbs of symbiont-containing non-leguminous plants and the Hbs in the roots of symbiont-free plants.(ABSTRACT TRUNCATED AT 400 WORDS)
摘要
  1. 目前已知的非脊椎动物血红蛋白(Hb)和肌红蛋白(Mb)的140多种氨基酸序列可分为几个不同的组:(1)单链球蛋白,含有一个血红素结合结构域;(2)截短的单链单结构域球蛋白;(3)嵌合的单结构域球蛋白;(4)嵌合的双结构域球蛋白;(5)嵌合的多结构域球蛋白。2. 已知8种非脊椎动物Hb和Mb的晶体结构,它们均为单体单结构域球蛋白链。尽管这些分子代表植物、原核生物和几个后生动物类群,尽管二聚体和四聚体分子中的亚基间相互作用与脊椎动物Hb中观察到的不同,但所有7种单结构域球蛋白的二级结构都保留了典型的脊椎动物“肌红蛋白折叠”。尚未确定代表其他四组的球蛋白的晶体结构。3. 此外,许多单结构域、双结构域和多结构域球蛋白链参与了广泛的四级结构,范围从同二聚体和异二聚体到分子量大于3000 kDa的高度复杂的多亚基聚集体(S. N. 维诺格拉多夫,《比较生物化学与生理学》82B,1 - 15,1985)。4. (1)单链单结构域球蛋白在大小上与脊椎动物球蛋白相当,且分布最广。(A)细胞内Hb包括:(i)多毛纲动物甘油虫的单体和多聚体Hb;(ii)螠虫海豆芽的四聚体Hb;(iii)诸如拟刺参和刺参等棘皮动物的二聚体Hb;(iv)软体动物双壳类的二聚体和四聚体Hb,如船蛆、泥蚶、横帘蛤和格氏蛤。(B)细胞外Hb包括:(i)昆虫摇蚊幼虫的多种单体和二聚体Hb;(ii)线虫如毛圆线虫和秀丽隐杆线虫的Hb;(iii)形成四聚体和十二聚体的球蛋白链,约占环节动物(如寡毛纲动物蚯蚓和多毛纲动物缨鳃虫)以及须腕动物管栖蠕虫巨大的(约3600 kDa)六边形双层(HBL)Hb的2 / 3;(iv)构成管栖蠕虫和须腕动物寡腕虫约400 kDa Hb的球蛋白链。(C)细胞质Hb包括:(i)软体动物腹足纲动物海兔、囊舌海牛、蟹守螺、织纹螺和多彩海牛以及石鳖的Mb;(ii)共生双壳类动物光亮海笋的三种Hb;(iii)细菌透明颤菌的二聚体Hb;(iv)植物Hb包括含共生体的豆科植物的Hb(Lgbs)、含共生体的非豆科植物的Hb以及不含共生体植物根中的Hb。(摘要截于400字)

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