The mini-hemoglobins in neural and body wall tissue of the nemertean worm, Cerebratulus lacteus

被引:42
作者
Vandergon, TL [1 ]
Riggs, CK
Gorr, TA
Colacino, JM
Riggs, AF
机构
[1] Univ Texas, Dept Zool, Austin, TX 78712 USA
[2] Clemson Univ, Dept Biol Sci, Clemson, SC 29631 USA
关键词
D O I
10.1074/jbc.273.27.16998
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Hemoglobin (Hb) occurs in circulating red blood cells, neural tissue, and body wall muscle tissue of the nemertean worm, Cerebratubus lacteus. The neural and body wall tissue each express single major Hb components for which the amino acid sequences have been deduced from cDNA and genomic DNA. These 109-residue globins form the smallest stable Hbs known. The globin genes have three exons and two introns with splice sites in the highly conserved positions of most globin genes. Alignment of the sequences with those of other globins indicates that the A, B, and H helices are about one-half the typical length. Phylogenetic analysis indicates that shortening results in a small tendency of globins to group together regardless of their actual relationships. The neural and body wall Hbs in situ are half-saturated with O-2 at 2.9 and 4.1 torr, respectively. The Hill coefficient for the neural Hb in situ, similar to 2.8, suggests that the neural Hb self-associates in the deoxy state at least to tetramers at the 2-3 mM (heme) concentration estimated in the cells. The Hb must dissociate upon oxygenation and dilution because the weight-average molecular mass of the HbO(2) in vitro is only about 18 kDa at 2-3 mu M heme concentration. Calculations suggest that the Hb can function as an O-2 store capable of extending neuronal activity in an anoxic environment for 5-30 min.
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页码:16998 / 17011
页数:14
相关论文
共 87 条
[1]   PHYSIOLOGICAL ADAPTATIONS IN DIVING VERTEBRATES [J].
ANDERSEN, HT .
PHYSIOLOGICAL REVIEWS, 1966, 46 (02) :212-+
[2]   INTRON-LESS GLOBIN GENES IN THE INSECT CHIRONOMUS-THUMMI-THUMMI [J].
ANTOINE, M ;
NIESSING, J .
NATURE, 1984, 310 (5980) :795-798
[3]   GLYCERA-DIBRANCHIATA HEMOGLOBIN - STRUCTURE AND REFINEMENT AT 1.5-A RESOLUTION [J].
ARENTS, G ;
LOVE, WE .
JOURNAL OF MOLECULAR BIOLOGY, 1989, 210 (01) :149-161
[4]   QUANTIFICATION OF TERTIARY STRUCTURAL CONSERVATION DESPITE PRIMARY SEQUENCE DRIFT IN THE GLOBIN FOLD [J].
ARONSON, HEG ;
ROYER, WE ;
HENDRICKSON, WA .
PROTEIN SCIENCE, 1994, 3 (10) :1706-1711
[5]  
ARVANITAKI A, 1960, B I OCEANOG, V57, P1
[6]  
ATKINSON HJ, 1975, J EXP BIOL, V62, P1
[7]   DETERMINANTS OF A PROTEIN FOLD - UNIQUE FEATURES OF THE GLOBIN AMINO-ACID-SEQUENCES [J].
BASHFORD, D ;
CHOTHIA, C ;
LESK, AM .
JOURNAL OF MOLECULAR BIOLOGY, 1987, 196 (01) :199-216
[8]  
Bevington R., 1969, DATA REDUCTION ERROR
[9]   STUDIES ON CONCENTRATION OF MYOGLOBIN IN SEA-COW AND PORPOISE [J].
BLESSING, MH .
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY, 1972, 41 (3A) :475-&
[10]  
Bonaventura J., 1973, COMP PHYSL, P493