Health in China. From Mao to market reform.

After the Liberation by Mao Ze Dong''s Communist army in 1949, China experienced massive social and economic change. The dramatic reductions in mortality and morbidity of the next two decades were brought about through improvements in socioeconomic conditions, an emphasis on prevention, and almost universal access to basic health care. The economic mismanagement of the Great Leap Forward brought about a temporary reversal in these positive trends. During the Cultural Revolution there was a sustained attack on the privileged position of the medical profession. Most city doctors were sent to work in the countryside, where they trained over a million barefoot doctors. Deng Xiao Ping''s radical economic reforms of the late 1970s replaced the socialist system with a market economy. Although average incomes have increased, the gap between rich and poor has widened.     

HhaI and HpaII DNA methyltransferases bind DNA mismatches, methylate uracil and block DNA repair.

The hydrolytic deamination of 5-methylcytosine (5-mC) to thymine (T) is believed to be responsible for the high mutability of the CpG dinucleotide in DNA. We have shown a possible alternate mechanism for mutagenesis at CpG in which HpaII DNA-(cytosine-5) methyltransferase (M.HpaII) can enzymatically deaminate cytosine (C) to uracil (U) in DNA [Shen, J.-C., Rideout, W.M., III and Jones, P.A., Cell, 71, 1073-1080, (1992)]. Both the hydrolytic deamination of 5-mC and enzymatic deamination of C create premutagenic DNA mismatches (G:U and G:T) with the guanine (G) originally paired to the normal C. Surprisingly, we found that DNA-(cytosine-5) methyltransferases have higher affinities for these DNA mismatches than for their normal G:C targets and are capable of transferring a methyl group to the 5-position of U, creating T at low efficiencies. This binding by methyltransferase to mismatches at the recognition site prevented repair of G:U mismatches by uracil DNA glycosylase in vitro.     

C to T and/or G to A transitions are responsible for loss of a MspI restriction site at the 5′-end of the human apolipoprotein AI gene

We detected the loss of a MspI restriction site by a C to T transition at +83 bp and a G to A transition at +84 bp of the 5-end non-coding region of the human apolipoprotein AI gene. This base change occurred at the hot spot (CCGG) for methylation, which may be important in the regulation of gene expression. The population frequency for the loss of the MspI site is 6.1%.     

Discrete differences between strains of different Rhizobium spp. for competitive nodule occupancy on beans

Rhizobium etli strain TAL182 and R. leguminosarum bv phaseoli strain 8002, both of which produce melanin pigment, were tested for their nodulation competitiveness on beans by paired inoculation with two strains which do not produce melanin: R. tropici strain CIAT899 and Rhizobium sp. strain TAL1145. An assay was developed to distinguish nodules formed by the melanin-producing and non-producing strains. Strain TAL182 had discrete competitive superiority over CIAT899 and TAL1145 for nodulation of beans. Nodulation competitiveness was not correlated with the ability to produce melanin pigment or the host range of the Rhizobium strains tested.The authors are with the Department of Plant Molecular Physiology, University of Hawaii, 3050 Maile Way, Gillmore 402, Honolulu, HI 96822, USA     

A missense mutation (G197→A) in theα-l-fucosidase gene of fucosidosis patients leads to loss ofα-l-fucosidase

Fucosidosis is an autosomal recessive lysosomal storage disease resulting from the absence of -l-fucosidase activity. Two natural missense mutations (G¹⁹⁷A) and (A⁸⁶⁰G) within the -l-fucosidase gene have been reported to be homozygous in four patients with fucosidosis. Expression of wild-type and mutated -l-fucosidase cDNAs in COS-1 cells revealed complete deficiency of -l-fucosidase for the G¹⁹⁷A transition and a normal level of enzyme for A⁸⁶⁰G. We therefore conclude that the change of G¹⁹⁷A is responsible for fucosidosis in the patients while A⁸⁶⁰G is a normal polymorphic variant of -l-fucosidase.     

The shape of myosin subfragment-1. A equivalent oblate ellipsoid model based on hydrodynamic properties

The molecular weights of the two heads of myosin subfragment-1, S-1(A1) and S-1(A2), based on sedimentation equilibrium are 120 000 and 110 000. Hydrodynamically, the two heads are indistinguishable, with intrinsic viscosity, [eta], of 0.064-0.065 dL/g and sedimentation coefficient, s(0)20,w, of 5.8 S.Together with the rotational correlation time taken from the literature (235 ns), all three hydrodynamic properties can be better fitted with an equivalent oblate ellipsoid of revolution than a prolate model. The width of the equatorial axis of the ellipsoid is about 135 A (the axial ratio is about 6). Probably, the S-1(A1) and S-1(A2) molecules have a half-doughnutlike or a flattened pearlike shape rather than an elongated one.     

Maximum likelihood estimation of growth yields

This work is concerned with statistical methods to estimate yield and maintenance parameters associated with microbial growth. For a given dilution rate, an experimenter typically measures substrate concentration, oxygen utilization rate, the rate of carbon dioxide evolution, and biomass concentration. These correlated response variables each contain information about the maintenance and yield parameters of interest. A maximum likelihood estimator which combines this correlated information for the yield and maintenance parameters is proposed, evaluated, and tested on literature data. Both point and interval estimators are considered.     

Methionine synthesis from 3-methylthioribose in apple tissue

The primary fate of 5-methylthioribose in apple tissue is the formation of methionine. Using dual labeled 5-methylthioribose, it was shown that both the CH₃S- group and the ribose portion of 5-methylthioribose were equally incorporated into methionine. Thus, the pathway involves modification of the ribose portion of 5-methylthioribose into the 2-aminobutyrate portion of methionine. This pathway functions to recycle methionine for continued synthesis of ethylene in fruit tissues. The methionine cycle in relation to ethylene biosynthesis is presented.