Sex Work and its Linkages with Informal Labour Markets in India: Findings from the First Pan-India Survey of Female Sex Workers

Based on the results of the First Pan India Survey of Female Sex Workers (n=3000), this paper positions sex work within the broader spectrum of informal labour markets that women engage with in India. It puts forth an important dimension missing so far in sex work studies in India – of sex workers with prior or simultaneous labour market work experience. Informal labour markets act as important sites/junctures linking poverty with sex work. For a substantial proportion of respondents, sex work was not their first experience of paid work. In the face of poverty and an early quest for livelihoods, they were pushed into informal labour activities, characterised by low, sticky wages and imminent possibilities of abuse. Placed in this context, their later entry into sex work emerges with a strong economic rationale and agency, as a deliberate, calculated choice offering higher incomes

A simple characterization of special matchings in lower Bruhat intervals

We give a simple characterization of special matchings in lower Bruhat intervals (that is, intervals starting from the identity element) of a Coxeter group. As a byproduct, we obtain some results on the action of special matchings.Comment: accepted for publication on Discrete Mathematic

Unique motifs identify PIG-A proteins from glycosyltransferases of the GT4 family

<p>Abstract</p> <p>Background</p> <p>The first step of GPI anchor biosynthesis is catalyzed by PIG-A, an enzyme that transfers <it>N</it>-acetylglucosamine from UDP-<it>N</it>-acetylglucosamine to phosphatidylinositol. This protein is present in all eukaryotic organisms ranging from protozoa to higher mammals, as part of a larger complex of five to six 'accessory' proteins whose individual roles in the glycosyltransferase reaction are as yet unclear. The PIG-A gene has been shown to be an essential gene in various eukaryotes. In humans, mutations in the protein have been associated with paroxysomal noctural hemoglobuinuria. The corresponding PIG-A gene has also been recently identified in the genome of many archaeabacteria although genes of the accessory proteins have not been discovered in them. The present study explores the evolution of PIG-A and the phylogenetic relationship between this protein and other glycosyltransferases.</p> <p>Results</p> <p>In this paper we show that out of the twelve conserved motifs identified by us eleven are exclusively present in PIG-A and, therefore, can be used as markers to identify PIG-A from newly sequenced genomes. Three of these motifs are absent in the primitive eukaryote, <it>G. lamblia</it>. Sequence analyses show that seven of these conserved motifs are present in prokaryote and archaeal counterparts in rudimentary forms and can be used to differentiate PIG-A proteins from glycosyltransferases. Using partial least square regression analysis and data involving presence or absence of motifs in a range of PIG-A and glycosyltransferases we show that (i) PIG-A may have evolved from prokaryotic glycosyltransferases and lipopolysaccharide synthases, members of the GT4 family of glycosyltransferases and (ii) it is possible to uniquely classify PIG-A proteins versus glycosyltransferases.</p> <p>Conclusion</p> <p>Besides identifying unique motifs and showing that PIG-A protein from <it>G. lamblia </it>and some putative PIG-A proteins from archaebacteria are evolutionarily closer to glycosyltransferases, these studies provide a new method for identification and classification of PIG-A proteins.</p

<i><span style="font-size:14.0pt;line-height: 115%;font-family:"Times New Roman";mso-fareast-font-family:"Times New Roman"; color:black;mso-ansi-language:EN-IN;mso-fareast-language:EN-IN;mso-bidi-language: HI" lang="EN-IN">In vitro</span></i><span style="font-size:14.0pt;line-height: 115%;font-family:"Times New Roman";mso-fareast-font-family:"Times New Roman"; color:black;mso-ansi-language:EN-IN;mso-fareast-language:EN-IN;mso-bidi-language: HI" lang="EN-IN"> plantlet regeneration from seedling nodal explants of <i>Acacia catechu</i></span>

1050-1055<span style="font-size:14.0pt;line-height: 115%;font-family:" times="" new="" roman";mso-fareast-font-family:"times="" roman";="" color:black;mso-ansi-language:en-in;mso-fareast-language:en-in;mso-bidi-language:="" hi"="" lang="EN-IN">Multiple shoots were initiated after 20 days in stem nodes excised from in vitro grown seedlings of Acacia catechu, on Murashige and Skoog's medium adjuvanted with 1 to 100 μM of N6-benzyladenine (B A). Explants were subcultured <span style="font-size:14.0pt; line-height:115%;font-family:" times="" new="" roman";mso-fareast-font-family:fd1433539-identity-h;="" color:black;mso-ansi-language:en-in;mso-fareast-language:en-in;mso-bidi-language:="" hi"="" lang="EN-IN">on <span style="font-size:14.0pt;line-height:115%; font-family:" times="" new="" roman";mso-fareast-font-family:"times="" roman";="" color:black;mso-ansi-language:en-in;mso-fareast-language:en-in;mso-bidi-language:="" hi"="" lang="EN-IN">the same medium augmented with 1.5 gl-1 of polyvinylpyrrolidone (PVP) after 30 days. In the second subculture, after 30 days, the explants were transferred to a medium lacking PVP, but containing 10 μM of BA, where nine or ten shoots differentiated per explant within next 30 days. If individual shoots along with some callus were subcultured on BA (10 μM), nearly 15 shoots per explant regenerated in 90 days. Thus, the average number of shoots obtained from each node was 142 after 180days. Since a seedling develops four nodes after 20 days, theoretically an average of 568 shoots can be obtained from a <span style="font-size:14.0pt;line-height: 115%;font-family:" times="" new="" roman";mso-fareast-font-family:fd1433539-identity-h;="" color:black;mso-ansi-language:en-in;mso-fareast-language:en-in;mso-bidi-language:="" hi"="" lang="EN-IN">sin<span style="font-size:14.0pt;line-height:115%; font-family:" times="" new="" roman";mso-fareast-font-family:"times="" roman";="" color:black;mso-ansi-language:en-in;mso-fareast-language:en-in;mso-bidi-language:="" hi"="" lang="EN-IN">gle seed. If shoots were individually subcultured on 1/2-strength MS medium with 14.7 μM of indole-3-butyric acid (IBA),roots developed in 20 days. Addition of 40 mgl-1of glutamic acid to the rooting medium prevented leaf senescence. These plantlets thrived well in garden soil, sand and silica (1:1:1).</span

Transformation of oilseed mustard <i style="">Brassica juncea</i> (L.) Czern & Coss cv. Pusajaikisan with snowdrop lectin gene

97-102An efficient protocol has been developed to transfer snowdrop lectin gene (gna) to Brassica juncea (L.) Czern & Coss cv. Pusajaikisan through Agrobacterium tumefaciens GV 2260 mediated transformation. High frequency regeneration of transformed plantlets has been achieved by using stem segments as explants. Analysis of the putative transformants by PCR amplification and Southern hybridization of genomic DNA showed the successful integration of the transgene in the nuclear genome. The transgenic plants will be further tested for bioassay in future

Breakout Session 2 - Labor Struggles

Breakout Session 2 - Labor Struggles Jillian Jacklin, University of Wisconsin, Madison, A Family Affair: Women, Children, and the Daily Work of Dairy Farmer Radicalism Mercedes Townsend, Sarah Lawrence College, \u27Venus to the Hoop,’ but Not to the Bank: Gender Inequity in Professional Basketball Tara Martin Lopez, Peninsula College, Retail Feminism: Working Class Women’s Fight for Equal Pay at Wal-Mart and ASDA V. Kalya Shankar and Rohini Sahni, The New School, Waste Pickers and the ‘Right to Waste’ in an Indian Cit

Unique motifs identify PIG-A proteins from glycosyltransferases of the GT4 family-8

appears to be closer to the archaeal proteins than to other eukaryotic PIG-A proteins.<p><b>Copyright information:</b></p><p>Taken from "Unique motifs identify PIG-A proteins from glycosyltransferases of the GT4 family"</p><p>http://www.biomedcentral.com/1471-2148/8/168</p><p>BMC Evolutionary Biology 2008;8():168-168.</p><p>Published online 4 Jun 2008</p><p>PMCID:PMC2446393.</p><p></p

Unique motifs identify PIG-A proteins from glycosyltransferases of the GT4 family-6

. Three of these motifs are absent in .<p><b>Copyright information:</b></p><p>Taken from "Unique motifs identify PIG-A proteins from glycosyltransferases of the GT4 family"</p><p>http://www.biomedcentral.com/1471-2148/8/168</p><p>BMC Evolutionary Biology 2008;8():168-168.</p><p>Published online 4 Jun 2008</p><p>PMCID:PMC2446393.</p><p></p

Unique motifs identify PIG-A proteins from glycosyltransferases of the GT4 family-7

Rged away from other eukaroyotic PIG-A proteins.<p><b>Copyright information:</b></p><p>Taken from "Unique motifs identify PIG-A proteins from glycosyltransferases of the GT4 family"</p><p>http://www.biomedcentral.com/1471-2148/8/168</p><p>BMC Evolutionary Biology 2008;8():168-168.</p><p>Published online 4 Jun 2008</p><p>PMCID:PMC2446393.</p><p></p

Unique motifs identify PIG-A proteins from glycosyltransferases of the GT4 family-1

Rged away from other eukaroyotic PIG-A proteins.<p><b>Copyright information:</b></p><p>Taken from "Unique motifs identify PIG-A proteins from glycosyltransferases of the GT4 family"</p><p>http://www.biomedcentral.com/1471-2148/8/168</p><p>BMC Evolutionary Biology 2008;8():168-168.</p><p>Published online 4 Jun 2008</p><p>PMCID:PMC2446393.</p><p></p