A P-Loop-Related Motif (GxxGxxK) Highly Conserved in Sulfotransferases Is Required for Binding the Activated Sulfate Donor

Komatsu, Katsutoshi; Driscoll, William J.; Koh, Youngchul; Strott, Charles A.

doi:10.1006/bbrc.1994.2587

Cited by 58 publications

(41 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…GXXGXXK motif at the C-terminal end of STs [8,9]. Site-directed mutagenesis within this region (GISGDWKN) in the guinea pig estrogen sulfotransferase markedly affected the Km for PAPS and confirmed this part of the amino acid sequence to be a critical component of the active site [9].…”

Section: Chemico-biological Interactionsmentioning

confidence: 83%

“…However, the change at position 235 in HAST4v compared to HAST4 involves a conservative substitution of an Asn for a Thr. This change is in close proximity to the putative PAPS binding domain [3,8,9] and resides within a region that shows subtle differences in amino acid differences between HAST1, HAST3 and HAST4 proteins. From Table 1 it is apparent that by attaching the last 120 amino acids of HAST4v to HAST4 it was possible to produce a protein that has a Km for PAPS similar to HAST4v.…”

Section: Chimeric Constructs Of Hast4 and Hast4vmentioning

confidence: 97%

“…The recent cloning of an increasing number of sulfotransferases from a variety of species and analysis of their amino acid sequences has revealed at least four highly conserved regions [2,7]. A number of laboratories have now utilised this data to construct chimeric cDNAs and perform site-directed mutagenesis on these regions, as well as carry out affinity labelling to gain insight into the substrate and PAPS binding sites of guinea pig [8,9], rat [10] and plant [7,11] STs. It has been suggested that the PAPS binding region resides in a highly conserved…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Structural and functional characterisation of human sulfotransferases

Brix

Nicoll

Zhu

et al. 1998

Chemico-Biological Interactions

View full text Add to dashboard Cite

The human aryl sulfotransferases HAST4 and HAST4v vary by only two amino acids but exhibit markedly different affinity towards the sulfonate acceptor p-nitrophenol and the sulfonate donor 3%-phosphoadenosine-5%-phosphosulfate (PAPS). To determine the importance of each of these amino acid differences, chimeric constructs were made of HAST4 and HAST4v. By attaching the last 120 amino acids of HAST4v to HAST4 (changing Thr235 to Asn235) we have been able to produce a protein that has a Km for PAPS similar to HAST4v. The reverse construct, HAST4v:4 produces a protein with a Km for PAPS similar to HAST4. These data suggests that the COOH-terminal of sulfotransferases is involved in co-factor binding.

show abstract

Section: Chemico-biological Interactionsmentioning

confidence: 83%

Section: Chimeric Constructs Of Hast4 and Hast4vmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Structural and functional characterisation of human sulfotransferases

Brix

Nicoll

Zhu

et al. 1998

Chemico-Biological Interactions

View full text Add to dashboard Cite

show abstract

“…The translated product of the hBR-STL-1 transcript also contains several sequences that are conserved in many SULTs [12]. These include the 5h TYPKSGT sequence (residues 52-58) involved with 3h-phosphoadenosine 5h-phosphosulphate (PAPS) binding, the putative active-site histidine residue (residue 111), the internal ' YGSWXXH ' motif (residues 172-178 ; ' X ' denotes ' any other residue ') and 3h GXXWKXXFTV, reported to also be involved with PAPS binding [13,14]. Figure 3 shows the Northern-blot analysis of the expression of hBR-STL message in several human tissues.…”

Section: Figure 4 Comparison Of the Rt-pcr Product Generated From Hummentioning

confidence: 99%

Molecular cloning and expression of novel sulphotransferase-like cDNAs from human and rat brain

Falany

Xie

Wang

et al. 2000

Biochemical Journal

View full text Add to dashboard Cite

The sulphotransferase (SULT) gene family is involved with the conjugation of many small drugs, xenobiotics and endogenous compounds. In this report, we describe the cloning and expression of novel cDNAs from human and rat brain, which are structurally related to the SULTs. These cDNAs have been termed ‘brain sulphotransferase-like’ (BR-STL), because of their similarity to the SULTs and their selective expression in brain tissue. The proteins encoded by the human and rat BR-STL cDNAs (hBR-STL-1 and rBR-STL cDNA respectively), denoted as hBR-STL and rBR-STL, are 98% identical and 99% similar in sequence. The hBR-STL-1 cDNA contains an 852-nt open reading frame encoding a 284-amino-acid protein with a calculated molecular mass of 33083 Da. Northern-blot analyses of RNA isolated from eight human tissues indicate that the hBR-STL message is selectively expressed in brain. Characterization of different brain regions showed that message levels were highest in cortical brain regions. rBR-STL message levels were relatively low in brains of 1-day-old male and female rats, but increased to adult levels in RNA from 7-day-old rats, and remained at that level in adult animals. The hBR-STL and rBR-STL cDNAs were expressed in both Escherichia coli and Sf9 insect cells in the presence or absence of an N-terminal histidine-affinity tag (His-tag). Polyclonal antibodies were raised in chickens against purified His-tagged hBR-STL, and were used to detect the presence of rBR-STL in adult male and female rat brain cytosol. The high degree of sequence conservation, and the selective localization of the BR-STL message in brain, suggest an important function in the central nervous system.

show abstract

“…1,3 These regions of sequence are important in binding the cosubstrate sulfate donor molecule 3 0 -phosphoadenosine 5 0 -phosphosulfate (PAPS). [4][5][6] In addition, Region IV forms part of the dimerization interface region for these enzymes. 7 SULTs can be classified into families whose members share at least 45% amino-acid sequence identity, and subfamilies that include enzymes that share at least 60% amino-acid sequence identity.…”

Section: Introductionmentioning

confidence: 99%

Human cytosolic sulfotransferase database mining: identification of seven novel genes and pseudogenes

et al. 2003

View full text Add to dashboard Cite

A total of 10 SULT genes are presently known to be expressed in human tissues. We performed a comprehensive genome-wide search for novel SULT genes using two different but complementary approaches, and developed a novel graphical display to aid in the annotation of the hits. Seven novel human SULT genes were identified, five of which were predicted to be pseudogenes, including two processed pseudogenes and three pseudogenes that contained introns. Those five pseudogenes represent the first unambiguous SULT pseudogenes described in any species. Expression-profiling studies were conducted for one novel gene, SULT6B1, and a series of alternatively spliced transcripts were identified in the human testis. SULT6B1 was also present in chimpanzee and gorilla, differing at only seven encoded amino-acid residues among the three species. The results of these database mining studies will aid in studies of the regulation of these SULT genes, provide insights into the evolution of this gene family in humans, and serve as a starting point for comparative genomic studies of SULT genes.

show abstract

A P-Loop-Related Motif (GxxGxxK) Highly Conserved in Sulfotransferases Is Required for Binding the Activated Sulfate Donor

Cited by 58 publications

References 0 publications

Structural and functional characterisation of human sulfotransferases

Structural and functional characterisation of human sulfotransferases

Molecular cloning and expression of novel sulphotransferase-like cDNAs from human and rat brain

Human cytosolic sulfotransferase database mining: identification of seven novel genes and pseudogenes

Contact Info

Product

Resources

About