02481caa  2200445   4500001000800000005001700008008004100025040000800066072000900074072000900083100001300092245015200105300001600257504002400273520120900297650002501506650002201531650001201553650002001565650001701585650001901602650001901621650001501640650003101655650001501686650001401701650001101715650002301726650002501749653002701774653002801801700001501829700002001844700002201864700001601886773007801902852001901980945002501999946001102024362144820040426152525.0040419e200401  |||           000 0 eng    aAGL 0aF600 0aF2001 aRoth, C.10aCharacterization of a protein of the plastid inner envelope having homology to animal inorganic phosphate, chloride and organic-anion transporters.  ap. 406-416.  aIncludes references  aA protein from Arabidopsis thaliana (L.) Heynh. showing homology to animal proteins of the NaPi-1 family, involved in the transport of inorganic phosphate, chloride, glutamate and sialic acid, has been characterized. This protein, named ANTR2 (for anion transporters) was shown by chloroplast subfractionation to be localized to the plastid inner envelope in both A. thaliana and Spinacia oleracea (L.). Immunolocalization revealed that ANTR2 was expressed in the leaf mesophyll cells as well as in the developing embryo at the upturned-U stage. Five additional homologues of ANTR2 are found in the Arabidopsis genome, of which one was shown by green fluorescent protein (GFP) fusion to be also located in the chloroplast. All ANTR proteins share homology to the animal NaPi-1 family, as well as to other organic-anion transporters that are members of the Anion:Cation Symporter (ACS) family, and share the main features of transporters from this family, including the presence of 12 putative transmembrane domains and of a 7-amino acid motif in the fourth putative transmembrane domain. ANTR2 thus represent a novel protein of the plastid inner envelope that is likely to be involved in anion transport. 3aArabidopsis thaliana 3aSpinacia oleracea 3aspinach 3avegetable crops 3achloroplasts 3acell membranes 3aplant proteins 3asymporters 3agene expression regulation 3aphosphates 3achlorides 3aanions 3asequence alignment 3aamino acid sequences  aanion:cation symporter  amolecular sequence data1 aMenzel, G.1 aPetetot, J.M.C.1 aRochat-Hacker, S.1 aPoirier, Y.0 tPlanta.g2004 Jan.,  v. 218, no. 3o1022630324x0032-09357nnas9jnl46291  aDNALi450 P693  aINDdRSCe2004/04/26  aNon-US02786caa  2200457   4500001000800000005001700008008004100025040000800066072000900074072000900083100002600092245016100118300001600279504002400295520145100319650001101770650001401781650001401795650001601809650001901825650001501844650003901859650002501898650002501923650002401948650002701972653002401999653002002023653001602043653002202059653002802081700001302109700001502122700001602137700001802153700001802171773008302189852002002272945002502292946001102317361563420040315080203.0040310e200402  |||           000 0 eng    aAGL 0aF200 0aF6001 aWeiss-Schneeweiss, H.10aChromosome termini of the monocot plant Othocallis siberica are maintained by telomerase, which specifically synthesises vertebrate-type telomere sequences.  ap. 484-493.  aIncludes references  aLack of Arabidopsis-type T3AG3 telomere sequences has recently been reported for the majority of investigated taxa of the monocot order Asparagales. In order to investigate this phenomenon in more detail, we conducted extensive cytogenetic and molecular analyses of the telomeres in Othocallis siberica, a member of this order. Terminal restriction fragment analysis together with Bal31 exonuclease assay showed that chromosome termini in O. siberica are formed by long stretches (more than 10 kbp) of vertebrate-type T2AG3 repeats. In addition, telomerase activity specifically synthesising (T2AG3)n sequence was detected in O. siberica protein extracts by telomerase repeat amplification protocol (TRAP). Fluorescence in situ hybridisation (FISH) revealed the presence of the vertebrate-type T2AG3 telomere sequences at all chromosome termini and at a few additional regions of O. siberica chromosomes, whereas Arabidopsis-type T3AG3 DNA and peptide nucleic acid (PNA) probes did not hybridise to chromosomes of Othocallis, except for polymorphic blocks in chromosomes 2 (interstitial) and 4 (terminal). These interstitial/terminal regions are apparently composed of large blocks of (T2AG3)n and (T3AG3)n DNA and represent a unique example of interspersion of two types of telomeric repeats within one genome. This may be a reflection of the recent evolutionary switch from Arabidopsis- to vertebrate-type telomeric repeats in this plant group. 3aScilla 3aLiliaceae 3atelomeres 3achromosomes 3aplant proteins 3atelomerase 3afluorescence in situ hybridization 3acytogenetic analysis 3anucleotide sequences 3arestriction mapping 3aendodeoxyribonucleases  aOthocallis siberica  aScilla siberica  aAsparagales  aBAL31 exonuclease  amolecular sequence data1 aRiha, K.1 aJang, C.G.1 aPuizina, J.1 aScherthan, H.1 aSchweizer, D.0 tPlant journal.g2004 Feb., v. 37, no. 4o1022630165x0960-74127nnas9jnl47643  aDNALiQK710.P68  aINDdRSCe2004/03/15  aNon-US